1v1b
From Proteopedia
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==Overview== | ==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, ... | + | 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== | ==About this Structure== | ||
| - | 1V1B is a | + | 1V1B 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 ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V1B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:06:40 2007'' |
Revision as of 12:01, 5 November 2007
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2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS WITH BOUND ATP
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
1V1B is a Single protein structure of sequence from Thermus thermophilus with ATP as ligand. Structure known Active Site: AC1. 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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