PDBsum entry: 1o0x

Hydrolase

PDB id: 1o0x

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

Protein chain

Q9X1I7  (Q9X1I7_THEMA) -  Methionine aminopeptidase

Seq: 250 a.a.

Struc: 249 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.11.18 - Methionyl aminopeptidase.
• Reaction: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
• Cofactor: Cobalt

 Gene Ontology (GO) functional annotation 

• Biological process: cellular process (2 terms)
• Biochemical function: hydrolase activity (5 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.