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PDBsum entry 1o0x

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protein links
Hydrolase PDB id
1o0x
Jmol
Contents
Protein chain
249 a.a. *
Waters ×195
* Residue conservation analysis
PDB id:
1o0x
Name: Hydrolase
Title: Crystal structure of methionine aminopeptidase (tm1478) from thermotoga maritima at 1.90 a resolution
Structure: Methionine aminopeptidase. Chain: a. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm1478. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.90Å     R-factor:   0.203     R-free:   0.254
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
G.Spraggon et al. (2004). Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution. Proteins, 56, 396-400. PubMed id: 15211524 DOI: 10.1002/prot.20084
Date:
13-Sep-02     Release date:   06-Nov-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9X1I7  (Q9X1I7_THEMA) -  Methionine aminopeptidase
Seq:
Struc:
250 a.a.
249 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.11.18  - Methionyl aminopeptidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
      Cofactor: Cobalt cation
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   2 terms 
  Biochemical function     hydrolase activity     6 terms  

 

 
DOI no: 10.1002/prot.20084 Proteins 56:396-400 (2004)
PubMed id: 15211524  
 
 
Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution.
G.Spraggon, R.Schwarzenbacher, A.Kreusch, D.McMullan, L.S.Brinen, J.M.Canaves, X.Dai, A.M.Deacon, M.A.Elsliger, S.Eshagi, R.Floyd, A.Godzik, C.Grittini, S.K.Grzechnik, L.Jaroszewski, C.Karlak, H.E.Klock, E.Koesema, J.S.Kovarik, P.Kuhn, T.M.McPhillips, M.D.Miller, A.Morse, K.Moy, J.Ouyang, R.Page, K.Quijano, F.Rezezadeh, A.Robb, E.Sims, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, F.von Delft, X.Wang, B.West, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, S.A.Lesley, I.A.Wilson.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Crystal structure of TM1478. (A) Ribbon diagram of Thermotoga maritima TM1478 color coded from N-terminus (blue) to C-terminus (red) showing the domain organization and the location of the active site (arrow). elices (H1-H6) and -strands ( 1- 14) are indicated. (B) Diagram showing the secondary structure elements in TM1478 superimposed on its primary sequence with -hairpins depicted in red and -sheets labeled in red as A-D.
Figure 2.
Figure 2. (A) Ribbon diagram of a superposition of TM1478 (cyan) and MAP from E. coli (grayish; PDB code: 1MAT). The active site residues are shown in ball and stick. (B) Close-up of the active site using superposition shown in (A). For comparison, the dinuclear cobalt center, its coordinating residues, and a bound methionine, as observed in the MAP structure from E. coli, are shown in ball and stick with carbon atoms colored gray, residue labels shown in brackets, and coordinating bonds to the metal shown in yellow dashes. The corresponding residues in TM1478 are depicted with their carbon atoms colored cyan.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 56, 396-400) copyright 2004.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19660503 J.J.Alvarado, A.Nemkal, J.M.Sauder, M.Russell, D.E.Akiyoshi, W.Shi, S.C.Almo, and L.M.Weiss (2009).
Structure of a microsporidian methionine aminopeptidase type 2 complexed with fumagillin and TNP-470.
  Mol Biochem Parasitol, 168, 158-167.
PDB codes: 3fm3 3fmq 3fmr
18952013 S.Mitra, B.Bennett, and R.C.Holz (2009).
Mutation of H63 and its catalytic affect on the methionine aminopeptidase from Escherichia coli.
  Biochim Biophys Acta, 1794, 137-143.  
19198897 S.Mitra, G.Sheppard, J.Wang, B.Bennett, and R.C.Holz (2009).
Analyzing the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosus.
  J Biol Inorg Chem, 14, 573-585.  
18369189 C.J.McCleverty, L.Columbus, A.Kreusch, and S.A.Lesley (2008).
Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634.
  Protein Sci, 17, 869-877.
PDB codes: 2vkj 2vko
18855426 S.J.Watterson, S.Mitra, S.I.Swierczek, B.Bennett, and R.C.Holz (2008).
Kinetic and spectroscopic analysis of the catalytic role of H79 in the methionine aminopeptidase from Escherichia coli.
  Biochemistry, 47, 11885-11893.  
19019076 S.Mitra, K.M.Job, L.Meng, B.Bennett, and R.C.Holz (2008).
Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.
  FEBS J, 275, 6248-6259.  
17064285 S.B.Conners, E.F.Mongodin, M.R.Johnson, C.I.Montero, K.E.Nelson, and R.M.Kelly (2006).
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
  FEMS Microbiol Rev, 30, 872-905.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.