1v1a
From Proteopedia
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| - | [[Image:1v1a.gif|left|200px]]<br /><applet load="1v1a" size=" | + | [[Image:1v1a.gif|left|200px]]<br /><applet load="1v1a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1v1a, resolution 2.10Å" /> | caption="1v1a, resolution 2.10Å" /> | ||
'''2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND 2-KETO-3-DEOXYGLUCONATE AND ADP'''<br /> | '''2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND 2-KETO-3-DEOXYGLUCONATE AND ADP'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with KDG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Adp Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1V1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=KDG:'>KDG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Adp+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:16:44 2008'' |
Revision as of 08:16, 3 February 2008
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2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND 2-KETO-3-DEOXYGLUCONATE AND ADP
Overview
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, 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.
About this Structure
1V1A is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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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