1DIK

PYRUVATE PHOSPHATE DIKINASE

Summary for 1DIK

• Entry DOI: 10.2210/pdb1dik/pdb
• Related: 2R82
• Descriptor: PYRUVATE PHOSPHATE DIKINASE, SULFATE ION (3 entities in total)
• Functional Keywords: transferase, kinase, phosphotransferase
• Biological source: Clostridium symbiosum
• Total number of polymer chains: 1
• Total formula weight: 97073.56

Authors

Herzberg, O.,Chen, C.C.H. (deposition date: 1995-12-06, release date: 1996-04-03, Last modification date: 2024-02-07)

Primary citation

Herzberg, O.,Chen, C.C.,Kapadia, G.,McGuire, M.,Carroll, L.J.,Noh, S.J.,Dunaway-Mariano, D.
Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites.
Proc.Natl.Acad.Sci.USA, 93:2652-2657, 1996

PubMed Abstract: The crystal structure of pyruvate phosphate dikinase, a histidyl multiphosphotransfer enzyme that synthesizes adenosine triphosphate, reveals a three-domain molecule in which the phosphohistidine domain is flanked by the nucleotide and the phosphoenolpyruvate/pyruvate domains, with the two substrate binding sites approximately 45 angstroms apart. The modes of substrate binding have been deduced by analogy to D-Ala-D-Ala ligase and to pyruvate kinase. Coupling between the two remote active sites is facilitated by two conformational states of the phosphohistidine domain. While the crystal structure represents the state of interaction with the nucleotide, the second state is achieved by swiveling around two flexible peptide linkers. This dramatic conformational transition brings the phosphocarrier residue in close proximity to phosphoenolpyruvate/pyruvate. The swiveling-domain paradigm provides an effective mechanism for communication in complex multidomain/multiactive site proteins.

PubMed: 8610096
DOI: 10.1073/pnas.93.7.2652

Experimental method

X-RAY DIFFRACTION (2.3 Å)