1un8
From Proteopedia
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| - | [[Image:1un8. | + | [[Image:1un8.jpg|left|200px]]<br /><applet load="1un8" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1un8" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1un8, resolution 2.50Å" /> | caption="1un8, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE OF C. FREUNDII (NATIVE FORM)'''<br /> | '''CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE OF C. FREUNDII (NATIVE FORM)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii] with MYY as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerone_kinase Glycerone kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.29 2.7.1.29] | + | 1UN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii] with MYY as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerone_kinase Glycerone kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.29 2.7.1.29] Known structural/functional Site: <scene name='pdbsite=AC1:Myy Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UN8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: kinase]] | [[Category: kinase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:04:07 2007'' |
Revision as of 15:54, 18 December 2007
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CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE OF C. FREUNDII (NATIVE FORM)
Overview
Dihydroxyacetone kinases are a sequence-conserved family of enzymes, which, utilize two different phosphoryldonors, ATP in animals, plants and some, bacteria, and a multiphosphoprotein of the phosphoenolpyruvate, carbohydrate phosphotransferase system in bacteria. Here we report the, 2.5-A crystal structure of the homodimeric Citrobacter freundii, dihydroxyacetone kinase complex with an ATP analogue and dihydroxyacetone., The N-terminal domain consists of two alpha/beta-folds with a molecule of, dihydroxyacetone covalently bound in hemiaminal linkage to the N epsilon 2, of His-220. The C-terminal domain consists of a regular eight-helix, alpha-barrel. The eight helices form a deep pocket, which includes a, tightly bound phospholipid. Only the lipid headgroup protrudes from the, surface. The nucleotide is bound on the top of the barrel across from the, entrance to the lipid pocket. The phosphate groups are coordinated by two, Mg2+ ions to gamma-carboxyl groups of aspartyl residues. The ATP binding, site does not contain positively charged or aromatic groups. Paralogues of, dihydroxyacetone kinase also occur in association with transcription, regulators and proteins of unknown function pointing to biological roles, beyond triose metabolism.
About this Structure
1UN8 is a Single protein structure of sequence from Citrobacter freundii with MYY as ligand. Active as Glycerone kinase, with EC number 2.7.1.29 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain., Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B, J Biol Chem. 2003 Nov 28;278(48):48236-44. Epub 2003 Sep 9. PMID:12966101
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