In silico identification and characterization of the ion transport specificity for P-type ATPases in the Mycobacterium tuberculosis complex

BMC Structural Biology

Volumn 12, Issue , 2012, Pages

  Novoa Aponte, Lorena ^a,d   León Torres, Andrés ^a,d   Patiño Ruiz, Miyer ^a,d   Cuesta Bernal, Jenifer ^a,d   Salazar, Luz Mary ^a,d   Landsman, David ^b   Mariño Ramírez, Leonardo ^b,c   Soto, Carlos Yesid ^a,d  

^a UNIVERSIDAD NACIONAL DE COLOMBIA   (Colombia)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

^c PanAmerican Bioinformatics Institute   (Colombia)

^d Ciudad Universitaria   (Colombia)

Author keywords

Conserved motifs; Ion transport; Mycobacterium tuberculosis complex; P type ATPases; Tuberculosis

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ALKALINE EARTH METAL; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; HEAVY METAL; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; METAL ION; P TYPE ADENOSINE TRIPHOSPHATASE; POTASSIUM PUMP; PROTEOME; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CELL MEMBRANE; ENZYME LOCALIZATION; HYDROPHOBICITY; ION TRANSPORT; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE SEQUENCE;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; COMPUTER SIMULATION; CONSERVED SEQUENCE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; ION TRANSPORT; IONS; MARKOV CHAINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TUBERCULOSIS;

BACILLI (CLASS); CORYNEBACTERINEAE; MYCOBACTERIUM TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS COMPLEX; PROKARYOTA;

EID: 84866839924     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-12-25     Document Type: Article

References (40)

1. WHO, Global tuberculosis control: WHO report 2011 Switzerland: Publications of the World Health Organization 2011 246
2. The role of IS6110 in the evolution of Mycobacterium tuberculosis. McEvoy CR, et al. Tuberculosis (Edinb) 2007 87 5 393 404 10.1016/j.tube.2007.05.010 (Pubitemid 47321897)
3. Detection and discrimination of Mycobacterium tuberculosis complex. Issa R, et al. Diagn Microbiol Infect Dis 2012 72 1 62 7 10.1016/j.diagmicrobio.2011. 09.021 22078904
4. Tuberculosis: pathophysiology, clinical features, and diagnosis. Knechel NA, Crit Care Nurse 2009 29 2 34 43 quiz 44 10.4037/ccn2009968 19339446
5. Latent tuberculosis: mechanisms of host and bacillus that contribute to persistent infection. Tufariello JM, Chan J, Flynn JL, Lancet Infect Dis 2003 3 9 578 90 10.1016/S1473-3099(03)00741-2 12954564 (Pubitemid 37064537)
6. The challenge of new drug discovery for tuberculosis. Koul A, et al. Nature 2011 469 7331 483 90 10.1038/nature09657 21270886
7. Comparative molecular biological analysis of membrane transport genes in organisms. Nagata T, et al. Plant Mol Biol 2008 66 6 565 85 10.1007/s11103-007- 9287-z 18293089
8. Evolution of substrate specificities in the P-type ATPase superfamily. Axelsen KB, Palmgren MG, J Mol Evol 1998 46 1 84 101 10.1007/PL00006286 9419228 (Pubitemid 28047242)
9. Transport ATPases into the year 2008: a brief overview related to types, structures, functions and roles in health and disease. Pedersen PL, J Bioenerg Biomembr 2007 39 5-6 349 55 18175209
10. Isolation and cloning of the K+-independent, ouabain-insensitive Na+-ATPase. Rocafull MA, et al. Biochim Biophys Acta 2011 1808 6 1684 700 10.1016/j.bbamem.2011.02.010 21334305
11. Na+ ATPase activities in chela muscle of the euryhaline crab Neohelice granulata: differential response to environmental salinity. Pinoni SAL, A A, J Exp Mar Bio Ecol 2009 372 1-2 91 97
12. Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme Transitions between the Na-form and the K-form studied with tryptic digestion as a tool. Jorgensen PL, Biochim Biophys Acta 1975 401 3 399 415 10.1016/0005-2736(75)90239-4 126698
13. Structure and mechanism of Na, K-ATPase: functional sites and their interactions. Jorgensen PL, Hakansson KO, Karlish SJ, Annu Rev Physiol 2003 65 817 49 10.1146/annurev.physiol.65.092101.142558 12524462 (Pubitemid 38249178)
14. A structural model for the catalytic cycle of Ca(2+)-ATPase. Xu C, et al. J Mol Biol 2002 316 1 201 11 10.1006/jmbi.2001.5330 11829513 (Pubitemid 34729276)
15. P-type ATPases. Palmgren MG, Nissen P, Annu Rev Biophys 2011 40 243 66 10.1146/annurev.biophys.093008.131331 21351879
16. Biology, structure and mechanism of P-type ATPases. Kuhlbrandt W, Nat Rev Mol Cell Biol 2004 5 4 282 95 10.1038/nrm1354 15071553 (Pubitemid 38480609)
17. In and out of the cation pumps: P-type ATPase structure revisited. Bublitz M, et al. Curr Opin Struct Biol 2010 20 4 431 9 10.1016/j.sbi.2010.06. 007 20634056
18. Uniprot cited 2011; Available from: http://www.uniprot.org/
19. PRALINETM: a strategy for improved multiple alignment of transmembrane proteins. Pirovano W, Feenstra KA, Heringa J, Bioinformatics 2008 24 4 492 7 10.1093/bioinformatics/btm636 18174178 (Pubitemid 351256292)
20. Profile hidden Markov models. Eddy SR, Bioinformatics 1998 14 9 755 63 10.1093/bioinformatics/14.9.755 9918945 (Pubitemid 28552108)
21. I-TASSER server for protein 3D structure prediction. Zhang Y, BMC Bioinforma 2008 9 40 10.1186/1471-2105-9-40 (Pubitemid 351267364)
22. Bioinformatic characterization of P-type ATPases encoded within the fully sequenced genomes of 26 eukaryotes. Thever MD, Saier MH Jr, J Membr Biol 2009 229 3 115 30 10.1007/s00232-009-9176-2 19548020
23. The P-type ATPase superfamily. Chan H, et al. J Mol Microbiol Biotechnol 2010 19 1-2 5 104 20962537
24. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Cole ST, Nature 1998 393 537 10.1038/31159 9634230 (Pubitemid 28319235)
25. Mycobacterial p(1)-type ATPases mediate resistance to zinc poisoning in human macrophages. Botella H, et al. Cell Host Microbe 2011 10 3 248 59 10.1016/j.chom.2011.08.006 21925112
26. Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review). Bramkamp M, Altendorf K, Greie JC, Mol Membr Biol 2007 24 5-6 375 86 17710642 (Pubitemid 47290691)
27. A P-type ATPase importer that discriminates between essential and toxic transition metals. Lewinson O, Lee AT, Rees DC, Proc Natl Acad Sci U S A 2009 106 12 4677 82 10.1073/pnas.0900666106 19264958
28. Identification of Ion-Selectivity Determinants in Heavy-Metal Transport P1B-type ATPases. Argüello JM, J Membr Biol 2003 195 93 108 10.1007/s00232-003-2048-2 14692449 (Pubitemid 37243987)
29. The structure and function of heavy metal transport P1B ATPases. Argüello JM, Eren E, González-Guerrero M, Biometals 2007 20 233 248 10.1007/s10534-006-9055-6 17219055 (Pubitemid 46776570)
30. Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence. Argüello JM, Gonzalez-Guerrero M, Raimunda D, Biochemistry 2011 50 46 9940 9 10.1021/bi201418k 21999638
31. CtpV: a putative copper exporter required for full virulence of Mycobacterium tuberculosis. Ward SK, et al. Mol Microbiol 2010 77 5 1096 1110 10.1111/j.1365-2958.2010.07273.x 20624225
32. A P-type ATPase importer that discriminates between essential and toxic transition metals. Lewinson O, Lee AT, Rees DC, Proc Natl Acad Sci 2009 106 12 4677 4682 10.1073/pnas.0900666106 19264958
33. Futai M, Wada Y, Kaplan JH, Handbook of ATPases: Biochemistry, Cell Biology, Pathophysiology. 1 ed Weinheim: WILEY-VCH Verlag GmbH & Co. KGaA 2004
34. Transcriptional Adaptation of Mycobacterium tuberculosis within Macrophages: Insights into the Phagosomal Environment. Schnappinger D, et al. J Exp Med 2003 198 5 693 704 10.1084/jem.20030846 12953091 (Pubitemid 37087769)
35. Identification of Mycobacterium tuberculosis genes preferentially expressed during human infection. Kumar M, et al. Microb Pathog 2011 50 1 31 8 10.1016/j.micpath.2010.10.003 21035536
36. The use of microarray analysis to determine the gene expression profiles of Mycobacterium tuberculosis in response to anti-bacterial compounds. Waddell SJ, et al. Tuberculosis (Edinb) 2004 84 3-4 263 74 (Pubitemid 38857859)
37. The influence of reduced oxygen availability on pathogenicity and gene expression in Mycobacterium tuberculosis. Bacon J, et al. Tuberculosis (Edinb) 2004 84 3-4 205 17 (Pubitemid 38857853)
38. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Sherman DR, et al. Proc Natl Acad Sci U S A 2001 98 13 7534 9 10.1073/pnas.121172498 11416222 (Pubitemid 32567983)
39. The Mycobacterium tuberculosis dosRS two-component system is induced by multiple stresses. Kendall SL, et al. Tuberculosis (Edinb) 2004 84 3-4 247 55 (Pubitemid 38857857)
40. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. Voskuil MI, et al. J Exp Med 2003 198 5 705 13 10.1084/jem.20030205 12953092 (Pubitemid 37087770)