1dgk
From Proteopedia
(New page: 200px<br /> <applet load="1dgk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dgk, resolution 2.8Å" /> '''MUTANT MONOMER OF RE...) |
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caption="1dgk, resolution 2.8Å" /> | caption="1dgk, resolution 2.8Å" /> | ||
'''MUTANT MONOMER OF RECOMBINANT HUMAN HEXOKINASE TYPE I WITH GLUCOSE AND ADP IN THE ACTIVE SITE'''<br /> | '''MUTANT MONOMER OF RECOMBINANT HUMAN HEXOKINASE TYPE I WITH GLUCOSE AND ADP IN THE ACTIVE SITE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DGK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GLC, PO4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1DGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Hexokinase Hexokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.1 2.7.1.1] Full crystallographic information is available from [http:// | + | 1DGK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1DGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Hexokinase Hexokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.1 2.7.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: sugar kinase]] | [[Category: sugar kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:39:43 2008'' |
Revision as of 13:39, 15 February 2008
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MUTANT MONOMER OF RECOMBINANT HUMAN HEXOKINASE TYPE I WITH GLUCOSE AND ADP IN THE ACTIVE SITE
Contents |
Overview
Hexokinase I, the pacemaker of glycolysis in brain tissue, is composed of, two structurally similar halves connected by an alpha-helix. The enzyme, dimerizes at elevated protein concentrations in solution and in crystal, structures; however, almost all published data reflect the properties of a, hexokinase I monomer in solution. Crystal structures of mutant forms of, recombinant human hexokinase I, presented here, reveal the enzyme monomer, for the first time. The mutant hexokinases bind both glucose 6-phosphate, and glucose with high affinity to their N and C-terminal halves, and ADP, also with high affinity, to a site near the N terminus of the polypeptide, chain. Exposure of the monomer crystals to ADP in the complete absence of, glucose 6-phosphate reveals a second binding site for adenine nucleotides, at the putative active site (C-half), with conformational changes, extending 15 A to the contact interface between the N and C-halves. The, structures reveal distinct conformational states for the C-half and a, rigid-body rotation of the N-half, as possible elements of a, structure-based mechanism for allosteric regulation of catalysis.
Disease
Known disease associated with this structure: Hemolytic anemia due to hexokinase deficiency OMIM:[142600]
About this Structure
1DGK is a Single protein structure of sequence from Homo sapiens with , and as ligands. The following page contains interesting information on the relation of 1DGK with [The Glycolytic Enzymes]. Active as Hexokinase, with EC number 2.7.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation., Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB, J Mol Biol. 2000 Mar 3;296(4):1001-15. PMID:10686099
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