1g5c
From Proteopedia
(New page: 200px<br /><applet load="1g5c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5c, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1g5c.jpg|left|200px]]<br /><applet load="1g5c" size=" | + | [[Image:1g5c.jpg|left|200px]]<br /><applet load="1g5c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g5c, resolution 2.1Å" /> | caption="1g5c, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br /> | '''CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the "cab"-type beta class carbonic anhydrase from the | + | The structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum (Cab) has been determined to 2.1-A resolution using the multiwavelength anomalous diffraction phasing technique. Cab exists as a dimer with a subunit fold similar to that observed in "plant"-type beta class carbonic anhydrases. The active site zinc is coordinated by protein ligands Cys(32), His(87), and Cys(90), with the tetrahedral coordination completed by a water molecule. The major difference between plant- and cab-type beta class carbonic anhydrases is in the organization of the hydrophobic pocket. The structure reveals a Hepes buffer molecule bound 8 A away from the active site zinc, which suggests a possible proton transfer pathway from the active site to the solvent. |
==About this Structure== | ==About this Structure== | ||
| - | 1G5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with ZN, CA and EPE 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:// | + | 1G5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=EPE:'>EPE</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=1G5C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ferry, J | + | [[Category: Ferry, J G.]] |
| - | [[Category: Iverson, T | + | [[Category: Iverson, T M.]] |
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
| - | [[Category: Smith, K | + | [[Category: Smith, K S.]] |
[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:25 2008'' |
Revision as of 10:46, 21 February 2008
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CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
Overview
The structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum (Cab) has been determined to 2.1-A resolution using the multiwavelength anomalous diffraction phasing technique. Cab exists as a dimer with a subunit fold similar to that observed in "plant"-type beta class carbonic anhydrases. The active site zinc is coordinated by protein ligands Cys(32), His(87), and Cys(90), with the tetrahedral coordination completed by a water molecule. The major difference between plant- and cab-type beta class carbonic anhydrases is in the organization of the hydrophobic pocket. The structure reveals a Hepes buffer molecule bound 8 A away from the active site zinc, which suggests a possible proton transfer pathway from the active site to the solvent.
About this Structure
1G5C is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with , and as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the "cab"-type beta class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum., Strop P, Smith KS, Iverson TM, Ferry JG, Rees DC, J Biol Chem. 2001 Mar 30;276(13):10299-305. Epub 2000 Nov 28. PMID:11096105
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