PDBsum entry 1qzt

Transferase

PDB id: 1qzt

Contents

Protein chains

332 a.a. *

Ligands

SO4 ×11

Waters ×102

* Residue conservation analysis

PDB id:

1qzt

Name:

Transferase

Title:

Phosphotransacetylase from methanosarcina thermophila

Structure:

Phosphate acetyltransferase. Chain: a, b, c, d. Fragment: phosphotransacetylase. Synonym: phosphotransacetylase. Engineered: yes

Source:

Methanosarcina thermophila. Organism_taxid: 2210. Gene: pta. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

2.70Å R-factor: 0.249 R-free: 0.286

Authors:

P.P.Iyer,S.H.Lawrence,K.B.Luther,K.R.Rajashankar,H.P.Yennawar, J.G.Ferry,H.Schindelin

Key ref:

P.P.Iyer et al. (2004). Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila. Structure, 12, 559-567. PubMed id: 15062079 DOI: 10.1016/j.str.2004.03.007

Date:

17-Sep-03 Release date: 22-Jun-04

Protein chains

P38503  (PTAS_METTE) -  Phosphate acetyltransferase from Methanosarcina thermophila

Seq: 333 a.a.

Struc: 332 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.1.8 - phosphate acetyltransferase.
• Reaction: acetyl-CoA + phosphate = acetyl phosphate + CoA

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2004.03.007

Structure 12:559-567 (2004)

PubMed id: 15062079

Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila.

P.P.Iyer, S.H.Lawrence, K.B.Luther, K.R.Rajashankar, H.P.Yennawar, J.G.Ferry, H.Schindelin.

ABSTRACT

is ubiquitous in the carbon assimilation and energy-yielding pathways in anaerobic prokaryotes where it catalyzes the reversible transfer of the acetyl group from acetyl phosphate to CoA forming acetyl CoA and inorganic phosphate. The crystal structure of Pta from the methane-producing archaeon Methanosarcina thermophila, representing the first crystal structure of any Pta, was determined by multiwavelength anomalous diffraction at 2.7 A resolution. In solution and in the crystal, the enzyme forms a homodimer. Each monomer consists of two alpha/beta domains with a cleft along the domain boundary, which presumably contains the substrate binding sites. Comparison of the four monomers present in the asymmetric unit indicates substantial variations in the relative orientation of the two domains and the structure of the putative active site cleft. A search for structural homologs revealed the NADP(+)-dependent isocitrate and isopropylmalate dehydrogenases as the only homologs with a similar two-domain architecture.

Selected figure(s)

Figure 2.
Figure 2. The Pta Dimer and Conformational Changes in the Pta Monomer(A) Structure of the Pta AB-dimer from the P4[1] crystal form viewed along the dimer axis. One monomer is colored according to Figure 1B, whereas domains I and II of the other monomer are shown in yellow and red, respectively. The arrows highlight the consequences of the rotation of domains I in the context of the dimer.(B) Maximum conformational change between the four monomers. A superposition of domain II from the two most dissimilar monomers in the P4[1] crystal form is displayed. The rotation of domain I around the hinge created by residues 145 and 300 is illustrated by the double-headed arrow.(C) Surface representation of the open conformation (A monomer) with domain I in yellow and domain II in magenta, with the width of the cleft highlighted by arrows.(D) Surface representation of the closed conformation (B monomer) color coded as in (C) where the top half of the cleft is closed. (C), (D), and Figure 3A were produced with SPOCK (Christopher, 1998)

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 559-567) copyright 2004.

Figure was selected by an automated process.