1jcl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1jcl.gif|left|200px]] | + | [[Image:1jcl.gif|left|200px]] |
| - | + | ||
| - | '''OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION''' | + | {{Structure |
| + | |PDB= 1jcl |SIZE=350|CAPTION= <scene name='initialview01'>1jcl</scene>, resolution 1.05Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1JCL is a [ | + | 1JCL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JCL OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11598300 11598300] |
[[Category: Deoxyribose-phosphate aldolase]] | [[Category: Deoxyribose-phosphate aldolase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| Line 23: | Line 32: | ||
[[Category: alpha-beta tim barrel]] | [[Category: alpha-beta tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:01:34 2008'' |
Revision as of 10:01, 20 March 2008
| |||||||
| , resolution 1.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Deoxyribose-phosphate aldolase, with EC number 4.1.2.4 | ||||||
| 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
Page seeded by OCA on Thu Mar 20 12:01:34 2008
