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| - | [[Image:2fr5.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2fr5| PDB=2fr5 | SCENE= }} | | {{STRUCTURE_2fr5| PDB=2fr5 | SCENE= }} |
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| - | '''Crystal Structure of Mouse Cytidine Deaminase Complexed with Tetrahydrouridine'''
| + | ===Crystal Structure of Mouse Cytidine Deaminase Complexed with Tetrahydrouridine=== |
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| - | ==Overview==
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| - | Cytidine deaminase (CDA) is a zinc-dependent enzyme that catalyzes the deamination of cytidine or deoxycytidine to form uridine or deoxyuridine. Here we present the crystal structure of mouse CDA (MmCDA), complexed with either tetrahydrouridine (THU), 3-deazauridine (DAU), or cytidine. In the MmCDA-DAU complex, it clearly demonstrates that cytidine is distinguished from uridine by its 4-NH(2) group that acts as a hydrogen bond donor. In the MmCDA-cytidine complex, cytidine, unexpectedly, binds as the substrate instead of the deaminated product in three of the four subunits, and in the remaining subunit it binds as the product uridine. Furthermore, the charge-neutralizing Arg68 of MmCDA has also exhibited two alternate conformations, I and II. In conformation I, the only conformation observed in the other structurally known homotetrameric CDAs, Arg68 hydrogen bonds Cys65 and Cys102 to modulate part of their negative charges. However, in conformation II the side chain of Arg68 rotates about 130 degrees around the Cgamma-Cdelta bond and abolishes these hydrogen bonds. The lack of hydrogen bonding may indirectly weaken the zinc-product interaction by increased electron donation from cysteine to the zinc ion, suggesting a novel product-expelling mechanism. On the basis of known structures, structural analysis further reveals two subclasses of homotetrameric CDAs that can be identified according to the position of the charge-neutralizing arginine residue. Implications for CDA-RNA interaction have also been considered.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16784234}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16784234 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16784234}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tetrahydrouridine]] | | [[Category: Tetrahydrouridine]] |
| | [[Category: Zinc]] | | [[Category: Zinc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:13:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:42:32 2008'' |
Revision as of 12:42, 28 July 2008
Template:STRUCTURE 2fr5
Crystal Structure of Mouse Cytidine Deaminase Complexed with Tetrahydrouridine
Template:ABSTRACT PUBMED 16784234
About this Structure
2FR5 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse., Teh AH, Kimura M, Yamamoto M, Tanaka N, Yamaguchi I, Kumasaka T, Biochemistry. 2006 Jun 27;45(25):7825-33. PMID:16784234
Page seeded by OCA on Mon Jul 28 15:42:32 2008
