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| - | [[Image:1af2.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1af2| PDB=1af2 | SCENE= }} | | {{STRUCTURE_1af2| PDB=1af2 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE COMPLEXED WITH URIDINE'''
| + | ===CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE COMPLEXED WITH URIDINE=== |
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| - | ==Overview==
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| - | Crystal structures of the cytidine deaminase-uridine product complex prepared either by cocrystallizing enzyme with uridine or by diffusing cytidine into ligand-free crystals show that the product binds as a 4-ketopyrimidine. They reveal four additional features of the catalytic process. (1) A water molecule bound to a site previously observed to bind the incoming 4-NH2 group represents the site for the leaving ammonia molecule. The conserved Pro 128 accommodates both moieties by orienting the carbonyl group of the previous residue. (2) The Glu 104 carboxylate group rotates from its hydrogen bond to the O4 hydroxyl group in transition-state analog complexes, forming a new hydrogen bond to the leaving group moiety. Thus, after stabilizing the hydroxyl group in the transition state, Glu 104 transfers a proton from that group to the leaving amino group, promoting enol-to-keto isomerization of the product. (3) Difference Fourier comparisons with transition-state complexes indicate that the pyrimidine ring rotates toward the zinc by approximately 10 degrees. The active site thus "pulls" the ring and 4-NH2 group in opposite directions during catalysis. To preserve coplanarity of the 4-keto group with the pyrimidine ring, the N1-C1' glycosidic bond bends by approximately 19 degrees out of the ring plane. This distortion may "spring-load" the product complex and promote dissociation. Failure to recognize a similar distortion could explain an earlier crystallographic interpretation of the adenosine deaminase-inosine complex [Wilson, D. K., & Quiocho, F. A. (1994) Nat. Struct. Biol. 1, 691-694]. (4) The Zn-Sgamma132 bond, which lengthens in transition-state complexes, shortens as the O4 atom returns to a state of lower negative charge in the planar product, consistent with our previous proposal that this bond buffers the zinc bond valence, compensating buildup of negative charge on the oxygen nucleophile during catalysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9125497}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9125497 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9125497}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Proton transfer]] | | [[Category: Proton transfer]] |
| | [[Category: Strain]] | | [[Category: Strain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:11:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:42:44 2008'' |
Revision as of 13:42, 30 June 2008
Template:STRUCTURE 1af2
CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE COMPLEXED WITH URIDINE
Template:ABSTRACT PUBMED 9125497
About this Structure
1AF2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization., Xiang S, Short SA, Wolfenden R, Carter CW Jr, Biochemistry. 1997 Apr 22;36(16):4768-74. PMID:9125497
Page seeded by OCA on Mon Jun 30 16:42:44 2008
