1k70
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
==The Structure of Escherichia coli Cytosine Deaminase bound to 4-Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-one== | ==The Structure of Escherichia coli Cytosine Deaminase bound to 4-Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-one== | ||
| - | <StructureSection load='1k70' size='340' side='right' caption='[[1k70]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1k70' size='340' side='right'caption='[[1k70]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1k70]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1k70]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K70 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HPY:4-HYDROXY-3,4-DIHYDRO-1H-PYRIMIDIN-2-ONE'>HPY</scene></td></tr> |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k70 OCA], [https://pdbe.org/1k70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k70 RCSB], [https://www.ebi.ac.uk/pdbsum/1k70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k70 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CODA_ECOLI CODA_ECOLI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k70 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k70 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cytosine deaminase (CD) catalyzes the deamination of cytosine, producing uracil. This enzyme is present in prokaryotes and fungi (but not multicellular eukaryotes) and is an important member of the pyrimidine salvage pathway in those organisms. The same enzyme also catalyzes the conversion of 5-fluorocytosine to 5-fluorouracil; this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. The enzyme is of widespread interest both for antimicrobial drug design and for gene therapy applications against tumors. The structure of Escherichia coli CD has been determined in the presence and absence of a bound mechanism-based inhibitor. The enzyme forms an (alphabeta)(8) barrel structure with structural similarity to adenosine deaminase, a relationship that is undetectable at the sequence level, and no similarity to bacterial cytidine deaminase. The enzyme is packed into a hexameric assembly stabilized by a unique domain-swapping interaction between enzyme subunits. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile. Substrate binding involves a significant conformational change that sequesters the reaction complex from solvent. | ||
| - | + | ==See Also== | |
| - | + | *[[Deaminase 3D structures|Deaminase 3D structures]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | == | + | |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Black | + | [[Category: Black ME]] |
| - | [[Category: Ireton | + | [[Category: Ireton GC]] |
| - | [[Category: McDermott | + | [[Category: McDermott G]] |
| - | [[Category: Stoddard | + | [[Category: Stoddard BL]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
The Structure of Escherichia coli Cytosine Deaminase bound to 4-Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-one
| |||||||||||
