2vgi
From Proteopedia
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|PDB= 2vgi |SIZE=350|CAPTION= <scene name='initialview01'>2vgi</scene>, resolution 2.87Å | |PDB= 2vgi |SIZE=350|CAPTION= <scene name='initialview01'>2vgi</scene>, resolution 2.87Å | ||
|SITE= <scene name='pdbsite=AC1:Fbp+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Pga+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:K+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Chain+A'>AC4</scene>, <scene name='pdbsite=AC5:Fbp+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Pga+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:K+Binding+Site+For+Chain+B'>AC7</scene>, <scene name='pdbsite=AC8:Mn+Binding+Site+For+Chain+B'>AC8</scene>, <scene name='pdbsite=AC9:Fbp+Binding+Site+For+Chain+C'>AC9</scene>, <scene name='pdbsite=BC1:Pga+Binding+Site+For+Chain+C'>BC1</scene>, <scene name='pdbsite=BC2:K+Binding+Site+For+Chain+C'>BC2</scene>, <scene name='pdbsite=BC3:Mn+Binding+Site+For+Chain+C'>BC3</scene>, <scene name='pdbsite=BC4:Fbp+Binding+Site+For+Chain+D'>BC4</scene>, <scene name='pdbsite=BC5:Pga+Binding+Site+For+Chain+D'>BC5</scene>, <scene name='pdbsite=BC6:K+Binding+Site+For+Chain+D'>BC6</scene> and <scene name='pdbsite=BC7:Mn+Binding+Site+For+Chain+D'>BC7</scene> | |SITE= <scene name='pdbsite=AC1:Fbp+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Pga+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:K+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Mn+Binding+Site+For+Chain+A'>AC4</scene>, <scene name='pdbsite=AC5:Fbp+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Pga+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:K+Binding+Site+For+Chain+B'>AC7</scene>, <scene name='pdbsite=AC8:Mn+Binding+Site+For+Chain+B'>AC8</scene>, <scene name='pdbsite=AC9:Fbp+Binding+Site+For+Chain+C'>AC9</scene>, <scene name='pdbsite=BC1:Pga+Binding+Site+For+Chain+C'>BC1</scene>, <scene name='pdbsite=BC2:K+Binding+Site+For+Chain+C'>BC2</scene>, <scene name='pdbsite=BC3:Mn+Binding+Site+For+Chain+C'>BC3</scene>, <scene name='pdbsite=BC4:Fbp+Binding+Site+For+Chain+D'>BC4</scene>, <scene name='pdbsite=BC5:Pga+Binding+Site+For+Chain+D'>BC5</scene>, <scene name='pdbsite=BC6:K+Binding+Site+For+Chain+D'>BC6</scene> and <scene name='pdbsite=BC7:Mn+Binding+Site+For+Chain+D'>BC7</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2vgf|2VGF]], [[2vgb|2VGB]], [[2vgg|2VGG]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgi OCA], [http://www.ebi.ac.uk/pdbsum/2vgi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vgi RCSB]</span> | ||
}} | }} | ||
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[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
[[Category: Zanella, A.]] | [[Category: Zanella, A.]] | ||
| - | [[Category: FBP]] | ||
| - | [[Category: K]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: PGA]] | ||
[[Category: alternative splicing]] | [[Category: alternative splicing]] | ||
[[Category: disease mutation]] | [[Category: disease mutation]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:11:57 2008'' |
Revision as of 02:12, 31 March 2008
| |||||||
| , resolution 2.87Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , , , , , , , and | ||||||
| Ligands: | , , , | ||||||
| Activity: | Pyruvate kinase, with EC number 2.7.1.40 | ||||||
| Related: | 2VGF, 2VGB, 2VGG
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ERYTHROCYTE PYRUVATE KINASE: R486W MUTANT
Overview
Deficiency of human erythrocyte isozyme (RPK) is, together with glucose-6-phosphate dehydrogenase deficiency, the most common cause of the nonspherocytic hemolytic anemia. To provide a molecular framework to the disease, we have solved the 2.7 A resolution crystal structure of human RPK in complex with fructose 1,6-bisphosphate, the allosteric activator, and phosphoglycolate, a substrate analogue, and we have functionally and structurally characterized eight mutants (G332S, G364D, T384M, D390N, R479H, R486W, R504L, and R532W) found in RPK-deficient patients. The mutations target distinct regions of RPK structure, including domain interfaces and catalytic and allosteric sites. The mutations affect to a different extent thermostability, catalytic efficiency, and regulatory properties. These studies are the first to correlate the clinical symptoms with the molecular properties of the mutant enzymes. Mutations greatly impairing thermostability and/or activity are associated with severe anemia. Some mutant proteins exhibit moderate changes in the kinetic parameters, which are sufficient to cause mild to severe anemia, underlining the crucial role of RPK for erythrocyte metabolism. Prediction of the effects of mutations is difficult because there is no relation between the nature and location of the replaced amino acid and the type of molecular perturbation. Characterization of mutant proteins may serve as a valuable tool to assist with diagnosis and genetic counseling.
About this Structure
2VGI is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1LIX. Full crystallographic information is available from OCA.
Reference
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia., Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A, J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. PMID:11960989
Page seeded by OCA on Mon Mar 31 05:11:57 2008
Categories: Homo sapiens | Pyruvate kinase | Single protein | Abraham, D J. | Bianchi, P. | Chiarelli, L. | Dolzan, M. | Fortin, R. | Galizzi, A. | Mattevi, A. | Valentini, G. | Wang, C. | Zanella, A. | Alternative splicing | Disease mutation | Glycolysis | Kinase | Magnesium | Metal-binding | Phosphorylation | Polymorphism | Pyruvate | Pyruvate kinase in the active r-state | Transferase
