1bic
From Proteopedia
(New page: 200px<br /> <applet load="1bic" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bic, resolution 1.9Å" /> '''CRYSTALLOGRAPHIC ANA...) |
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| - | [[Image:1bic.gif|left|200px]]<br /> | + | [[Image:1bic.gif|left|200px]]<br /><applet load="1bic" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1bic" size=" | + | |
caption="1bic, resolution 1.9Å" /> | caption="1bic, resolution 1.9Å" /> | ||
'''CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-'''<br /> | '''CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically. Human isoenzyme II was | + | A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically. Human isoenzyme II was mutated at position 200 from threonine to histidine, which results in higher affinity for bicarbonate. The HCO3- ion binds in the active site to the zinc ion as a pseudo-bidentate ligand which gives the metal a coordination geometry between tetrahedral and trigonal bipyramide. The water/hydroxide normally bound with tetrahedral coordination to the zinc is probably replaced by the OH group of the bicarbonate ion. The importance of residues Thr-199 and Glu-106 in controlling the binding orientation of HCO3- is discussed as well as the catalytic mechanism. Both the complex as well as the uncomplexed mutant were studied at 1.9 A resolution. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BIC 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 ZN, BCT and MMC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http:// | + | 1BIC 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=ZN:'>ZN</scene>, <scene name='pdbligand=BCT:'>BCT</scene> and <scene name='pdbligand=MMC:'>MMC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jonsson, B | + | [[Category: Jonsson, B H.]] |
[[Category: Liljas, A.]] | [[Category: Liljas, A.]] | ||
[[Category: Lindskog, S.]] | [[Category: Lindskog, S.]] | ||
| - | [[Category: Svensson, L | + | [[Category: Svensson, L A.]] |
[[Category: Vidgren, J.]] | [[Category: Vidgren, J.]] | ||
[[Category: Xue, Y.]] | [[Category: Xue, Y.]] | ||
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[[Category: lyase(oxo-acid)]] | [[Category: lyase(oxo-acid)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:35 2008'' |
Revision as of 09:55, 21 February 2008
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CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-
Contents |
Overview
A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically. Human isoenzyme II was mutated at position 200 from threonine to histidine, which results in higher affinity for bicarbonate. The HCO3- ion binds in the active site to the zinc ion as a pseudo-bidentate ligand which gives the metal a coordination geometry between tetrahedral and trigonal bipyramide. The water/hydroxide normally bound with tetrahedral coordination to the zinc is probably replaced by the OH group of the bicarbonate ion. The importance of residues Thr-199 and Glu-106 in controlling the binding orientation of HCO3- is discussed as well as the catalytic mechanism. Both the complex as well as the uncomplexed mutant were studied at 1.9 A resolution.
Disease
Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]
About this Structure
1BIC is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-., Xue Y, Vidgren J, Svensson LA, Liljas A, Jonsson BH, Lindskog S, Proteins. 1993 Jan;15(1):80-7. PMID:8451242
Page seeded by OCA on Thu Feb 21 11:55:35 2008
Categories: Carbonate dehydratase | Homo sapiens | Single protein | Jonsson, B H. | Liljas, A. | Lindskog, S. | Svensson, L A. | Vidgren, J. | Xue, Y. | BCT | MMC | ZN | Lyase(oxo-acid)
