2vgi

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[[Image:2vgi.jpg|left|200px]]<br /><applet load="2vgi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2vgi.jpg|left|200px]]
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caption="2vgi, resolution 2.87&Aring;" />
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'''HUMAN ERYTHROCYTE PYRUVATE KINASE: R486W MUTANT'''<br />
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{{Structure
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|PDB= 2vgi |SIZE=350|CAPTION= <scene name='initialview01'>2vgi</scene>, resolution 2.87&Aring;
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|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>
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|LIGAND= <scene name='pdbligand=FBP:FRUCTOSE-1,6-DIPHOSPHATE'>FBP</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
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|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]
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|GENE=
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}}
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'''HUMAN ERYTHROCYTE PYRUVATE KINASE: R486W MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2VGI 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=FBP:'>FBP</scene>, <scene name='pdbligand=PGA:'>PGA</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1LIX. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGI OCA].
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2VGI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1LIX. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGI OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11960989 11960989]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11960989 11960989]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Pyruvate kinase]]
[[Category: Pyruvate kinase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:46:21 2008''

Revision as of 16:46, 20 March 2008

Image:2vgi.jpg


PDB ID 2vgi

Drag the structure with the mouse to rotate
, resolution 2.87Å
Sites: , , , , , , , , , , , , , , and
Ligands: , , and
Activity: Pyruvate kinase, with EC number 2.7.1.40
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

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