1jcl
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HPD:1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE'>HPD</scene> | |LIGAND= <scene name='pdbligand=HPD:1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE'>HPD</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase Deoxyribose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.4 4.1.2.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase Deoxyribose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.4 4.1.2.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jcj|1JCJ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jcl OCA], [http://www.ebi.ac.uk/pdbsum/1jcl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jcl RCSB]</span> | ||
}} | }} | ||
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[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: Wong, C H.]] | [[Category: Wong, C H.]] | ||
| - | [[Category: HPD]] | ||
[[Category: alpha-beta tim barrel]] | [[Category: alpha-beta tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:42 2008'' |
Revision as of 18:31, 30 March 2008
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| , resolution 1.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Deoxyribose-phosphate aldolase, with EC number 4.1.2.4 | ||||||
| Related: | 1JCJ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION
Overview
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.
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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