1v1s: Difference between revisions

Revision as of 14:23, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v1s.png

Template:STRUCTURE 1v1s

2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (CRYSTAL FORM 2)2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (CRYSTAL FORM 2)

Template:ABSTRACT PUBMED 15210349

About this StructureAbout this Structure

1V1S is a Single protein structure of sequence from Thermus thermophilus. 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

Page seeded by OCA on Tue Jul 29 14:23:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1v1s|  PDB=1v1s  |  SCENE=  }}
-'''2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (CRYSTAL FORM 2)'''
+===2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS (CRYSTAL FORM 2)===
-==Overview==
+<!--
--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, the TtKDGK structure with its KDG and ATP analogue was determined and refined at 2.1 angstroms. The bound KDG was observed predominantly as an open chain structure. The positioning of ligands and the conservation of important catalytic residues suggest that the reaction mechanism is likely to be similar to that of other members of the PfkB family, including ribokinase. In particular, the Asp251 is postulated to have a role in transferring the gamma-phosphate of ATP to the 5'-hydroxyl group of KDG.
+The line below this paragraph, {{ABSTRACT_PUBMED_15210349}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15210349 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15210349}}
 ==About this Structure==
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 [[Category: Thermus thermophilus]]
 [[Category: Transferase]]
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