Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis

Proteins: Structure, Function and Genetics

Volumn 70, Issue 1, 2008, Pages 273-279

  Nocek, B ^a   Mulligan, R ^a   Bargassa, M ^a   Collart, F ^a   Joachimiak, A ^a,b  

^a ARGONNE NATIONAL LABORATORY   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

Active site Zn ion binding; Aminopeptidase N; PepN; SAD phasing; Structural genomics

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; NEISSERIA MENINGITIDIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANTIGENS, CD13; BINDING SITES; CRYSTALLOGRAPHY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEISSERIA MENINGITIDIS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

NEISSERIA MENINGITIDIS;

EID: 37349116228     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21276     Document Type: Article

References (30)

1. Holz RC, Bzymek KP, Swierczek SI. Co-catalytic metallopeptidases as pharmaceutical targets. Curr Opin Chem Biol 2003;7:197-206.
2. Wilcox DE. Binuclear metallohydrolases. Chem Rev 1996;96:2435-2458.
3. Gonzales T, Robert-Baudouy J. Bacterial aminopeptidases: properties and functions. FEMS Microbiol Rev 1996;18:319-344.
4. Copik AJ, Nocek BP, Swierczek SI, Ruebush S, Jang SB, Meng L, D'Souza VM, Peters JW, Bennett B, Holz RC. EPR and X-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus. Biochemistry 2005;44:121-129.
5. Hooper NM. Families of zinc metalloproteases. FEBS Lett 1994;354:1-6.
6. Lowther WT, Matthews BW. Metalloaminopeptidases: common functional themes in disparate structural surroundings. Chem Rev 2002;102:4581-4608.
7. Rawlings ND, Barrett AJ. Evolutionary families of metallopeptidases. Methods Enzymol 1995;248:183-228.
8. Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA. Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli. Proc Natl Acad Sci USA 1998;95:3472-3477.
9. Rawlings ND, Tolle DP, Barrett AJ MEROPS: the peptidase database. Nucleic Acids Res 2004;32:D160-D164 (Database issue).
10. Noble F, Luciani N, Da Nascimento S, Lai-Kuen R, Bischoff L, Chen H, Fournie-Zaluski MC, Roques BP. Binding properties of a highly potent and selective iodinated aminopeptidase N inhibitor appropriate for radioautography. FEBS Lett 2000;467:81-86.
11. Tan PS, van Kessel TA, van de Veerdonk FL, Zuurendonk PF, Bruins AP, Konings WN. Degradation and debittering of a tryptic digest from beta-casein by aminopeptidase N from Lactococcus lactis subsp. cremoris Wg2. Appl Environ Microbiol 1993;59:1430-1436.
12. Walsh MA, Dementieva I, Evans G, Sanishvili R, Joachimiak A. Taking MAD to the extreme: ultrafast protein structure determination. Acta Crystallogr D Biol Crystallogr 1999;55 (Part 6):1168-1173.
13. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50 (Part 5):760-763.
14. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60 (Part 12, Part 1):2126-2132.
15. Laskowski RA, Moss DS, Thornton JM. Main-chain bond lengths and bond angles in protein structures. J Mol Biol 1993;231:1049-1067.
16. Krissinel E, Henrick K. Detection of protein assemblies in crystals. Lect Notes Comput Sci 2005;3695:163-174.
17. Thunnissen MM, Nordlund P, Haeggstrom JZ. Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation. Nat Struct Biol 2001;8:131-135.
18. Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
19. Kyrieleis OJ, Goettig P, Kiefersauer R, Huber R, Brandstetter H. Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations. J Mol Biol 2005;349:787-800.
20. Krissinel E, Henrick K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 2004;60 (Part 12, Part 1):2256-2268.
21. Binkowski TA, Joachimiak A, Liang J. Protein surface analysis for function annotation in high-throughput structural genomics pipeline. Protein Sci 2005;14:2972-2981.
22. Stols L, Gu M, Dieckman L, Raffen R, Collart FR, Donnelly MI. A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expr Purif 2002;25:8-15.
23. Kim Y, Dementieva I, Zhou M, Wu R, Lezondra L, Quartey P, Joachimiak G, Korolev O, Li H, Joachimiak A. Automation of protein purification for structural genomics. J Struct Funct Genomics 2004;5:111-118.
24. 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.
25. Stols L, Millard CS, Dementieva I, Donnelly MI. Production of selenomethionine-labeled proteins in two-liter plastic bottles for structure determination. J Struct Funct Genomics 2004;5:95-102.
26. Minor W, Cymborowski M, Otwinowski Z, Chruszcz M. HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes. Acta Crystallogr D Biol Crystallogr 2006;62 (Part 8):859-866.
27. Schneider TR, Sheldrick GM Substructure solution with SHELXD. Acta Crystallogr D Biol Crystallogr 2002;58 (Part 10, Part 2):1772-1779.
28. Terwilliger TC. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol 2003;374:22-37.
29. Perrakis A, Morris R, Lamzin VS. Automated protein model building combined with iterative structure refinement. Nat Struct Biol 1999;6:458-463.
30. Painter J, Merritt EA. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 2006;62 (Part 4):439-450.