1v1a: Difference between revisions
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Revision as of 17:13, 30 October 2007
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2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND 2-KETO-3-DEOXYGLUCONATE AND ADP
OverviewOverview
2-Keto-3-deoxygluconate kinase (KDGK) catalyzes the phosphorylation of, 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDGP)., The genome sequence of Thermus thermophilus HB8 contains an open reading, frame that has a 30% identity to Escherichia coli KDGK. The KDGK activity, of T.thermophilus protein (TtKDGK) has been confirmed, and its crystal, structure has been determined by the molecular replacement method and, refined with two crystal forms to 2.3 angstroms and 3.2 angstroms, respectively. The enzyme is a hexamer organized as a trimer of dimers., Each subunit is composed of two domains, a larger alpha/beta domain and a, smaller beta-sheet domain, similar to that of ribokinase and adenosine, kinase, members of the PfkB family of carbohydrate kinases. Furthermore, ... [(full description)]
About this StructureAbout this Structure
1V1A is a [Single protein] structure of sequence from [Thermus thermophilus] with KDG and ADP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of Thermus thermophilus 2-Keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate., Ohshima N, Inagaki E, Yasuike K, Takio K, Tahirov TH, J Mol Biol. 2004 Jul 9;340(3):477-89. PMID:15210349
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