PDBsum entry 3sdz

Hydrolase

PDB id

3sdz

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Contents

			Protein chain

					548 a.a.

			Ligands

					MPD ×6


					ACY ×6


					TRS ×3

			Waters ×273

PDB id:

3sdz

Links

Name:

Hydrolase

Title:

Structural characterization of the subunit a mutant f427w of the a-atp synthase from pyrococcus horikoshii

Structure:

V-type atp synthase alpha chain. Chain: a. Fragment: unp residues 1-240, 617-964. Synonym: a-type atp synthase catalytic subunit a, v-atpase subunit a. Engineered: yes. Mutation: yes. Other_details: the fusion protein of residues 1-240 and 617-964 of v- atpase subunit a

Source:

Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Gene: atpa, ph1975. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.53Å

R-factor:

0.203

R-free:

0.266

Authors:

V.S.Tadwal,M.S.S.Manimekalai,A.M.Balakrishna,G.Gruber

Key ref:

V.S.Tadwal et al. (2011). Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy. Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 1485-1491. PubMed id: 22139149 DOI: 10.1107/S1744309111039595

Date:

09-Jun-11

Release date:

25-Jan-12

PROCHECK

	Headers

	References

Protein chain

O57728 (VATA_PYRHO) - V-type ATP synthase alpha chain from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: Struc:

Seq: Struc:					964 a.a. 548 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

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



		Enzyme reactions

Enzyme class:

E.C.7.1.2.2 - H(+)-transporting two-sector ATPase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

ATP + H2O + 4 H⁺(in) = ADP + phosphate + 5 H⁺(out)

ATP	+	H2O	+	4 × H(+)(in)	=	ADP	+	phosphate	+	5 × H(+)(out)

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

reference

DOI no: 10.1107/S1744309111039595	Acta Crystallogr Sect F Struct Biol Cryst Commun 67:1485-1491 (2011)
PubMed id: 22139149

Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy.
V.S.Tadwal, M.S.Manimekalai, G.Grüber.

ABSTRACT

No abstract given.