PDBsum entry: 1g8r

Metal binding protein

PDB id: 1g8r

Contents

Protein chains

403 a.a. *

Ligands

GOL ×12

Waters ×206

* Residue conservation analysis

PDB id:

1g8r

Name:

Metal binding protein

Title:

Moea

Structure:

Molybdopterin biosynthesis moea protein. Chain: a, b

Source:

Escherichia coli. Organism_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

2.65Å R-factor: 0.221 R-free: 0.271

Authors:

S.Xiang,J.Nichols,K.V.Rajagopalan,H.Schindelin

Key ref:

S.Xiang et al. (2001). The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin. Structure, 9, 299-310. PubMed id: 11525167 DOI: 10.1016/S0969-2126(01)00588-3

Date:

20-Nov-00 Release date: 02-May-01

Protein chains

P12281  (MOEA_ECOLI) -  Molybdopterin molybdenumtransferase

Seq: 411 a.a.

Struc: 403 a.a.

Enzyme reactions

• Enzyme class: E.C.2.10.1.1 - Molybdopterin molybdotransferase.
• Reaction: Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP
• Cofactor: Zinc or magnesium

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

 Gene Ontology (GO) functional annotation 

• Biological process: molybdopterin cofactor biosynthetic process (2 terms)
• Biochemical function: protein binding (3 terms)

Key reference

DOI no: 10.1016/S0969-2126(01)00588-3

Structure 9:299-310 (2001)

PubMed id: 11525167

The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin.

S.Xiang, J.Nichols, K.V.Rajagopalan, H.Schindelin.

ABSTRACT

BACKGROUND: Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in archaea, eubacteria, and eukaryotes. In humans, genetic abnormalities in the biosynthetic pathway result in Moco deficiency, which is accompanied by severe neurological symptoms and death shortly after birth. The Escherichia coli MoeA and MogA proteins are involved in the final step of Moco biosynthesis: the incorporation of molybdenum into molybdopterin (MPT), the organic pyranopterin moiety of Moco. RESULTS: The crystal structure of E. coli MoeA has been refined at 2 A resolution and reveals that the highly elongated MoeA monomer consists of four clearly separated domains, one of which is structurally related to MogA, indicating a divergent evolutionary relationship between both proteins. The active form of MoeA is a dimer, and a putative active site appears to be localized to a cleft formed between domain II of the first monomer and domains III and IV of the second monomer. CONCLUSIONS: In eukaryotes, MogA and MoeA are fused into a single polypeptide chain. The corresponding mammalian protein gephyrin has also been implicated in the anchoring of glycinergic receptors to the cytoskeleton at inhibitory synapses. Based on the structures of MoeA and MogA, gephyrin is surmised to be a highly organized molecule containing at least five domains. This multidomain arrangement could provide a structural basis for its functional diversity. The oligomeric states of MoeA and MogA suggest how gephyrin could assemble into a hexagonal scaffold at inhibitory synapses.

Selected figure(s)

Figure 3.
Figure 3. Structural Similarities of Domains I, III, and IV(a) Superposition of domain III and MogA (Protein Data Base [PDB] entry 1DI6).(b) Superposition of domain I and the C-terminal domain of ornithine decarboxylase (PDB entry 1ORD).(c) Superposition of domain IV and the l phage display platform protein gdP (PDB entry 1C5E). All proteins are shown as ribbon diagrams with the different domains of MoeA colored according to Figure 2b and the structural matches in gray

The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 299-310) copyright 2001.

Figure was selected by an automated process.