1g5c

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{{STRUCTURE_1g5c| PDB=1g5c | SCENE= }}
{{STRUCTURE_1g5c| PDB=1g5c | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''
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===CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11096105 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11096105}}
==About this Structure==
==About this Structure==
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[[Category: Hepe]]
[[Category: Hepe]]
[[Category: Zinc]]
[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:27:07 2008''

Revision as of 01:27, 1 July 2008

Template:STRUCTURE 1g5c

CRYSTAL STRUCTURE OF THE 'CAB' TYPE BETA CLASS CARBONIC ANHYDRASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Template:ABSTRACT PUBMED 11096105

About this Structure

1G5C is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. 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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