PDBsum entry 3a1e

Hydrolase

PDB id: 3a1e

Contents

Protein chains

268 a.a. *

Ligands

ACP ×2

Metals

_MG

Waters ×317

* Residue conservation analysis

PDB id:

3a1e

Name:

Hydrolase

Title:

Crystal structure of the p- and n-domains of his462gln mutant copa, a copper-transporting p-type atpase, bound with amppcp-mg

Structure:

Probable copper-exporting p-type atpase a. Chain: a, b. Fragment: residues 387-673. Engineered: yes. Mutation: yes

Source:

Archaeoglobus fulgidus. Organism_taxid: 2234. Gene: copa, pacs, af_0473. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.95Å R-factor: 0.210 R-free: 0.245

Authors:

T.Tsuda,C.Toyoshima

Key ref:

T.Tsuda and C.Toyoshima (2009). Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase. Embo J, 28, 1782-1791. PubMed id: 19478797

Date:

31-Mar-09 Release date: 21-Jul-09

Protein chains

O29777  (COPA_ARCFU) -  Probable copper-exporting P-type ATPase from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 804 a.a.

Struc: 268 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.7.2.2.8 - P-type Cu(+) transporter.
• Reaction: Cu⁺(in) + ATP + H2O = Cu⁺(out) + ADP + phosphate + H⁺

Cu(+)(in) + ATP + H2O = Cu(+)(out) (Bound ligand (Het Group name = ACP) matches with 81.25% similarity) + ADP + phosphate + H(+)

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

reference

Embo J 28:1782-1791 (2009)

PubMed id: 19478797

Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase.

T.Tsuda, C.Toyoshima.

ABSTRACT

Heavy metal pumps constitute a large subgroup in P-type ion-transporting ATPases. One of the outstanding features is that the nucleotide binding N-domain lacks residues critical for ATP binding in other well-studied P-type ATPases. Instead, they possess an HP-motif and a Gly-rich sequence in the N-domain, and their mutations impair ATP binding. Here, we describe 1.85 A resolution crystal structures of the P- and N-domains of CopA, an archaeal Cu(+)-transporting ATPase, with bound nucleotides. These crystal structures show that CopA recognises the adenine ring completely differently from other P-type ATPases. The crystal structure of the His462Gln mutant, in the HP-motif, a disease-causing mutation in human Cu(+)-ATPases, shows that the Gln side chain mimics the imidazole ring, but only partially, explaining the reduction in ATPase activity. These crystal structures lead us to propose a role of the His and a mechanism for removing Mg(2+) from ATP before phosphoryl transfer.