1jcl

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[[Image:1jcl.gif|left|200px]]
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{{STRUCTURE_1jcl| PDB=1jcl | SCENE= }}
{{STRUCTURE_1jcl| PDB=1jcl | SCENE= }}
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'''OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION'''
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===OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION===
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==Overview==
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In classical enzymology, intermediates and transition states in a catalytic mechanism are usually inferred from a series of biochemical experiments. Here, we derive an enzyme mechanism from true atomic-resolution x-ray structures of reaction intermediates. Two ultra-high resolution structures of wild-type and mutant d-2-deoxyribose-5-phosphate (DRP) aldolase complexes with DRP at 1.05 and 1.10 angstroms unambiguously identify the postulated covalent carbinolamine and Schiff base intermediates in the aldolase mechanism. In combination with site-directed mutagenesis and (1)H nuclear magnetic resonance, we can now propose how the heretofore elusive C-2 proton abstraction step and the overall stereochemical course are accomplished. A proton relay system appears to activate a conserved active-site water that functions as the critical mediator for proton transfer.
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(as it appears on PubMed at http://www.pubmed.gov), where 11598300 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11598300}}
==About this Structure==
==About this Structure==
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[[Category: Wong, C H.]]
[[Category: Wong, C H.]]
[[Category: Alpha-beta tim barrel]]
[[Category: Alpha-beta tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:03:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:01:42 2008''

Revision as of 17:01, 1 July 2008

Template:STRUCTURE 1jcl

OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION

Template:ABSTRACT PUBMED 11598300

About this Structure

1JCL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Observation of covalent intermediates in an enzyme mechanism at atomic resolution., Heine A, DeSantis G, Luz JG, Mitchell M, Wong CH, Wilson IA, Science. 2001 Oct 12;294(5541):369-74. PMID:11598300

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