1h0c: Difference between revisions
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[[Image:1h0c.jpg|left|200px]]<br /><applet load="1h0c" size=" | [[Image:1h0c.jpg|left|200px]]<br /><applet load="1h0c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1h0c, resolution 2.50Å" /> | caption="1h0c, resolution 2.50Å" /> | ||
'''THE CRYSTAL STRUCTURE OF HUMAN ALANINE:GLYOXYLATE AMINOTRANSFERASE'''<br /> | '''THE CRYSTAL STRUCTURE OF HUMAN ALANINE:GLYOXYLATE AMINOTRANSFERASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1H0C 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 PLP, AOA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alanine--glyoxylate_transaminase Alanine--glyoxylate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44] Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 1H0C 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=PLP:'>PLP</scene>, <scene name='pdbligand=AOA:'>AOA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alanine--glyoxylate_transaminase Alanine--glyoxylate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.44 2.6.1.44] Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H0C OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
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Revision as of 10:44, 3 February 2008
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THE CRYSTAL STRUCTURE OF HUMAN ALANINE:GLYOXYLATE AMINOTRANSFERASE
OverviewOverview
A deficiency of the liver-specific enzyme alanine:glyoxylate, aminotransferase (AGT) is responsible for the potentially lethal, hereditary kidney stone disease primary hyperoxaluria type 1 (PH1). Many, of the mutations in the gene encoding AGT are associated with specific, enzymatic phenotypes such as accelerated proteolysis (Ser205Pro), intra-peroxisomal aggregation (Gly41Arg), inhibition of pyridoxal, phosphate binding and loss of catalytic activity (Gly82Glu), and, peroxisome-to-mitochondrion mistargeting (Gly170Arg). Several mutations, including that responsible for AGT mistargeting, co-segregate and interact, synergistically with a Pro11Leu polymorphism found at high frequency in, the normal population. In order to gain further insights into the, mechanistic link between genotype and enzymatic phenotype in PH1, we have, determined the crystal structure of normal human AGT complexed to the, competitive inhibitor amino-oxyacetic acid to 2.5A. Analysis of this, structure allows the effects of these mutations and polymorphism to be, rationalised in terms of AGT tertiary and quaternary conformation, and in, particular it provides a possible explanation for the Pro11Leu-Gly170Arg, synergism that leads to AGT mistargeting.
DiseaseDisease
Known diseases associated with this structure: Hyperoxaluria, primary, type 1 OMIM:[604285]
About this StructureAbout this Structure
1H0C is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Alanine--glyoxylate transaminase, with EC number 2.6.1.44 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1., Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ, J Mol Biol. 2003 Aug 15;331(3):643-52. PMID:12899834
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