PDBsum entry 1v4a

Transferase

PDB id: 1v4a

Contents

Protein chain

429 a.a. *

Waters ×171

* Residue conservation analysis

PDB id:

1v4a

Name:

Transferase

Title:

Structure of the n-terminal domain of escherichia coli glutamine synthetase adenylyltransferase

Structure:

Glutamate-ammonia-ligase adenylyltransferase. Chain: a. Fragment: n-terminal domain. Synonym: glutamine-synthetase adenylyltransferase, atase, adenylyltransferase. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.00Å R-factor: 0.230 R-free: 0.269

Authors:

Y.Xu,R.Zhang,A.Joachimiak,P.D.Carr,D.L.Ollis,S.G.Vasudevan

Key ref:

Y.Xu et al. (2004). Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure, 12, 861-869. PubMed id: 15130478 DOI: 10.1016/j.str.2004.02.029

Date:

12-Nov-03 Release date: 27-Jul-04

Protein chain

P30870  (GLNE_ECOLI) -  Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme from Escherichia coli (strain K12)

Seq: 946 a.a.

Struc: 429 a.a.

Enzyme reactions

• Enzyme class 1: E.C.2.7.7.42 - [glutamine synthetase] adenylyltransferase.
• Reaction: [glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O₄- (5'-adenylyl)-L-tyrosine + diphosphate
• Enzyme class 2: E.C.2.7.7.89 - [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase.
• Reaction: [glutamine synthetase]-O₄-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1016/j.str.2004.02.029

Structure 12:861-869 (2004)

PubMed id: 15130478

Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.

Y.Xu, R.Zhang, A.Joachimiak, P.D.Carr, T.Huber, S.G.Vasudevan, D.L.Ollis.

ABSTRACT

We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.

Selected figure(s)

Figure 4.
Figure 4. Ribbon Diagram of Overlay Domain 3 and KNTThe beginning and last residues of the domain 3 were labeled: AT-N440, cyan; KNT, orange.

The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 861-869) copyright 2004.

Figure was selected by an automated process.