X-Ray Crystal Structure of CutA from Thermotoga maritima at 1.4 Å Resolution

Proteins: Structure, Function and Genetics

Volumn 54, Issue 1, 2004, Pages 162-165

  Savchenko, Alexei ^a   Skarina, Tatiana ^a   Evdokimova, Elena ^a   Watson, James D ^d   Laskowski, Roman ^d   Arrowsmith, Cheryl H ^a,c   Edwards, Aled M ^a,b   Joachimiak, Andrzej ^e   Zhang, Rong Guang ^e  

^a UNIVERSITY HEALTH NETWORK   (Canada)

^b Banting and Best Department of Medical Research   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

^d UNIVERSITY OF LONDON   (United Kingdom)

^e ARGONNE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; BACTERIAL PROTEIN; METALLOPROTEIN; PROTEIN CUTA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CELL SURFACE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTAL STRUCTURE; DIFFRACTION; MAMMAL; MOLECULAR GENETICS; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; THERMOTOGA MARITIMA; WAVEFORM; X RAY ANALYSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; METALLOPROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; THERMOTOGA MARITIMA;

ARCHAEA; BACTERIA (MICROORGANISMS); MAMMALIA; THERMOTOGA; THERMOTOGA MARITIMA;

EID: 0348047618     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10585     Document Type: Article

References (21)

1. Fong ST, Camakaris J, Lee BT. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol Microbiol 1995;15:1127-1137.
2. Perrier AL, Cousin X, Boschetti N, Haas R, Chatel JM, Bon S, Roberts WL, Pickett SR, Massoulie J, Rosenberry TL, Krejci E. Two distinct proteins are associated with tetrameric acetylcholinesterase on the cell surface. J Biol Chem, 2000;275:34260-34265.
3. Holm L, Sander C. Dali: a network tool for protein structure comparison. Trends Biochem Sci 1995;20:478-480.
4. Orengo CA, Taylor WR. SSAP: sequential structure alignment program for protein structure comparison. Methods Enzymol 1996;266:617-635.
5. Cheah, E, Carr PD, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL. Structure of the Escherichia coli signal transducing protein PII. Structure 1994;2:981-990.
6. Xu, Y, Cheah E, Carr PD, van Heeswijk WC, Westerhoff HV, Vasudevan SG, Ollis DL. GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. J Mol Biol 1998;282:149-165.
7. Magasanik B. The regulation of nitrogen utilization in enteric bacteria. J Cell Biochem 1993;51:34-40.
8. Ninfa AJ, Atkinson MR. PII signal transduction proteins. Trends Microbiol 2000;8:172-179.
9. Arcondeguy T, Jack R, Merrick M. P(II) signal transduction proteins, pivotal players in microbial nitrogen control. Microbiol Mol Biol Rev 2001;65:80-105.
10. Kamberov ES, Atkinson MR, Ninfa AJ. The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP. J Biol Chem 1995;270:17797-17807.
11. Xu Y, Carr PD, Huber T, Vasudevan SG, Ollis DL. The structure of the PII-ATP complex. Eur J Biochem, 2001;268:2028-2037.
12. Martinez-Argudo I, Contreras A. PII T-loop mutations affecting signal transduction to NtrB also abolish yeast two-hybrid interactions. J Bacteriol 2002;184:3746-3748.
13. Gitschier J, Moffat B, Reilly D, Wood WI, Fairbrother WJ. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat Struct Biol 1998;5:47-54.
14. Rosenzweig, AC, Huffman DL, Hou MY, Wernimont AK, Pufahl RA, O'Halloran TV. Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution. Structure Fold Des 1999;7:605-617.
15. DiDonato M, Narindrasorasak S, Forbes JR, Cox DW, Sarkar B. Expression, purification, and metal binding properties of the N-terminal domain from the wilson disease putative copper-transporting ATPase (ATP7B). J Biol Chem 1997;272:33279-33282.
16. Lutsenko S, Petrukhin K, Cooper MJ, Gilliam CT, Kaplan JH. N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J Biol Chem 1997;272:18939-18944.
17. Zhang RG, Skarina T, Katz JE, Beasley S, Khachatryan A, Vyas S, Arrowsmith CH, Clarke S, Edwards A, Joachimiak A, Savchenko A. Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase. Structure (Camb), 2001;9:1095-1106.
18. Walsh MA, Evans G, Sanishvili R, Dementieva I, Joachimiak A. MAD data collection -current trends. Acta Crystallogr D Biol Crystallogr 1999;55:1726-1732.
19. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;307-326.
20. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998;54:905-921.
21. Perrakis A, Harkiolaki M, Wilson KS, Lamzin VS. ARP/wARP and molecular replacement. Acta Crystallogr D Biol Crystallogr 2001;57:1445-1450.