Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding

Protein Science

Volumn 20, Issue 2, 2011, Pages 406-416

  Matsuoka, Eriko ^a   Tanaka, Yoshikazu ^a   Kuroda, Makoto ^b   Shouji, Yuko ^a   Ohta, Toshiko ^c   Tanaka, Isao ^a   Yao, Min ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

^c UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

Crystal structure; Hemagglutination; MSCRAMMs; Staphylococcus saprophyticus; UafA

Indexed keywords

BACTERIAL PROTEIN; UNCLASSIFIED DRUG; URO ADHERENCE FACTOR A;

ARTICLE; BACTERIUM ADHERENCE; CRYSTAL STRUCTURE; CRYSTALLIZATION; ERYTHROCYTE; HEMAGGLUTINATION INHIBITION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STAPHYLOCOCCUS SAPROPHYTICUS; X RAY DIFFRACTION;

ADHESINS, BACTERIAL; ANIMALS; BINDING SITES; CELL ADHESION; ERYTHROCYTES; HEMAGGLUTINATION INHIBITION TESTS; LIGANDS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SHEEP; STAPHYLOCOCCUS SAPROPHYTICUS; X-RAY DIFFRACTION;

STAPHYLOCOCCUS; STAPHYLOCOCCUS SAPROPHYTICUS;

EID: 79251554358     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.573     Document Type: Article

References (35)

1. Torres Pereira A (1962) Coagulase-negative strains of staphylococcus possessing antigen 51 as agents of urinary infection. J Clin Pathol 15:252-253.
2. Meers PD, Whyte W, Sandys G (1975) Coagulase-negative staphylococci and micrococci in urinary tract infections. J Clin Pathol 28:270-273.
3. Wallmark G, Arremark I, Telander B (1978) Staphylococcus saprophyticus: a frequent cause of acute urinary tract infection among female outpatients. J Infect Dis 138:791-797.
4. Kahlmeter G (2003) An international survey of the antimicrobial susceptibility of pathogens from uncomplicated urinary tract infections: the ECO.SENS Project. J Antimicrob Chemother 51:69-76.
5. Raz R, Colodner R, Kunin CM (2005) Who are you-Staphylococcus saprophyticus? Clin Infect Dis 40:896-898.
6. von Eiff C, Peters G, Heilmann C (2002) Pathogenesis of infections due to coagulase-negative staphylococci. Lancet Infect Dis 2:677-685.
7. Patti JM, Hook M (1994) Microbial adhesins recognizing extracellular matrix macromolecules. Curr Opin Cell Biol 6:752-758.
8. Foster TJ, Hook M (1998) Surface protein adhesins of Staphylococcus aureus. Trends Microbiol 6:484-488.
9. Kuroda M, Ohta T, Uchiyama I, Baba T, Yuzawa H, Kobayashi I, Cui L, Oguchi A, Aoki K, Nagai Y, Lian J, Ito T, Kanamori M, Matsumaru H, Maruyama A, Murakami H, Hosoyama A, Mizutani-Ui Y, Takahashi NK, Sawano T, Inoue R, Kaito C, Sekimizu K, Hirakawa H, Kuhara S, Goto S, Yabuzaki J, Kanehisa M, Yamashita A, Oshima K, Furuya K, Yoshino C, Shiba T, Hattori M, Ogasawara N, Hayashi H, Hiramatsu K. (2001) Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357:1225-1240.
10. Kuroda M, Yamashita A, Hirakawa H, Kumano M, Morikawa K, Higashide M, Maruyama A, Inose Y, Matoba K, Toh H, Kuhara S, Hattori M, Ohta T. (2005) Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection. Proc Natl Acad Sci USA 102: 13272-13277.
11. Mazmanian SK, Ton-That H, Schneewind O (2001) Sortase-catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus. Mol Microbiol 40: 1049-1057. (Pubitemid 32574974)
12. Deivanayagam CC, Wann ER, Chen W, Carson M, Rajashankar KR, Hook M, Narayana SV (2002) A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A. EMBO J 21:6660-6672.
13. Ganesh VK, Rivera JJ, Smeds E, Ko YP, Bowden MG, Wann ER, Gurusiddappa S, Fitzgerald JR, Hook M (2008) A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. PLoS Pathog 4:e1000226.
14. Ponnuraj K, Bowden MG, Davis S, Gurusiddappa S, Moore D, Choe D, Xu Y, Hook M, Narayana SV (2003) A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen. Cell 115:217-228.
15. Bowden MG, Heuck AP, Ponnuraj K, Kolosova E, Choe D, Gurusiddappa S, Narayana SV, Johnson AE, Hook M (2008) Evidence for the "dock, lock, and latch" ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (MSCRAMM) SdrG. J Biol Chem 283: 638-647.
16. Zong Y, Xu Y, Liang X, Keene DR, Hook A, Gurusiddappa S, Hook M, Narayana SV (2005) A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen. EMBO J 24:4224-4236.
17. Deivanayagam CC, Rich RL, Carson M, Owens RT, Danthuluri S, Bice T, Hook M, Narayana SV (2000) Novel fold and assembly of the repetitive B region of the Staphylococcus aureus collagen-binding surface protein. Structure 8:67-78.
18. Rich RL, Demeler B, Ashby K, DeivanayagamCC, Petrich JW, Patti JM, Narayana SV, HookM(1998) Domain structure of the Staphylococcus aureus collagen adhesin. Biochemistry 37:15423-15433.
19. Deivanayagam CC, Perkins S, Danthuluri S, Owens RT, Bice T, Nanavathy T, Foster TJ, Hook M, Narayana SV (1999) Crystallization of ClfA and ClfB fragments: the fibrinogen-binding surface proteins of Staphylococcus aureus. Acta Cryst D55:554-556.
20. Luo BH, Carman CV, Springer TA (2007) Structural basis of integrin regulation and signaling. Annu Rev Immunol 25:619-647.
21. Tikkanen K, Haataja S, Francois-Gerard C, Finne J (1995) Purification of a galactosyl-alpha 1-4-galactosebinding adhesin from the gram-positive meningitisassociated bacterium Streptococcus suis. J Biol Chem 270:28874-28878.
22. Tikkanen K, Haataja S, Finne J (1996) The galactosyl-(alpha 1-4)-galactose-binding adhesin of Streptococcus suis: occurrence in strains of different hemagglutination activities and induction of opsonic antibodies. Infect Immun 64:3659-3665.
23. Jin R, Rummel A, Binz T, Brunger AT (2006) Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444:1092-1095.
24. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
25. Sheldrick GM, Hauptman HA, Weeks CM, Miller R, Uson I Ab initio phasing. In: Arnold E, Ed. (2001) International tables for crystallography, Vol. F. Dordrecht: Kluwer Academic Publishers, pp. 333-351.
26. Terwilliger TC, Berendzen J (1999) Automated MAD and MIR structure solution. Acta Cryst D55:849-861.
27. Terwilliger TC, Berendzen J (1999) Evaluation of macromolecular electron-density map quality using the correlation of local r.m.s. density. Acta Cryst D55:1872-1877.
28. Terwilliger TC (2000) Maximum-likelihood density modification. Acta Cryst D56:965-972.
29. Terwilliger TC (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Cryst D59:38-44.
30. Terwilliger TC (2003) Automated side-chain model building and sequence assignment by template matching. Acta Cryst D59:45-49.
31. Cowtan K (1994) Dm: an automated procedure for phase improvement by density modification. Joint CCP4 and ESFEACBM Newsletter on Protein Crystallography 31:34-38.
32. Yao M, Zhou Y, Tanaka I (2006) LAFIRE: software for automating the refinement process of protein-structure analysis. Acta Cryst D62:189-196.
33. Jones TA, Zou JY, Cowan SW, Kjeldgaard (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A47:110-119.
34. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximumlikelihood method. Acta Cryst D53:240-255.
35. Vagin A, Teplyako A (1997) MOLREP: an automated program for molecular replacement. J Appl Cryst 30: 1022-1025.