2w3u
From Proteopedia
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- | [[ | + | ==FORMATE COMPLEX OF THE NI-FORM OF E.COLI DEFORMYLASE== |
+ | <StructureSection load='2w3u' size='340' side='right' caption='[[2w3u]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2w3u]] is a 1 chain structure with 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=2W3U OCA]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1def|1def]], [[1lru|1lru]], [[1bs8|1bs8]], [[1bsk|1bsk]], [[2vhm|2vhm]], [[1bs7|1bs7]], [[2ai8|2ai8]], [[2def|2def]], [[1icj|1icj]], [[1bs4|1bs4]], [[1bs5|1bs5]], [[1bsz|1bsz]], [[2w3t|2w3t]], [[1dff|1dff]], [[1g2a|1g2a]], [[1g27|1g27]], [[1bs6|1bs6]], [[1dtf|1dtf]], [[1bsj|1bsj]], [[2dtf|2dtf]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w3u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w3u RCSB], [http://www.ebi.ac.uk/pdbsum/2w3u PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w3/2w3u_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Crystal structures of polypeptide deformylase (PDF) of Escherichia coli with nickel(II) replacing the native iron(II) have been solved with chloride and formate as metal ligands. The chloro complex is a model for the correct protonation state of the hydrolytic hydroxo ligand and the protonated status of the Glu133 side chain as part of the hydrolytic mechanism. The ambiguity that recently some PDFs have been identified with Zn(2+) ion as the active-site centre whereas others are only active with Fe(2+) (or Co(2+), Ni(2+) is discussed with respect to Lewis acid criteria of the metal ion and substrate activation by the CD loop. | ||
- | + | Structure of the Ni(II) complex of Escherichia coli peptide deformylase and suggestions on deformylase activities depending on different metal(II) centres.,Yen NT, Bogdanovic X, Palm GJ, Kuhl O, Hinrichs W J Biol Inorg Chem. 2010 Feb;15(2):195-201. PMID:20112455<ref>PMID:20112455</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Formylmethionine deformylase]] | [[Category: Formylmethionine deformylase]] |
Revision as of 08:43, 7 May 2014
FORMATE COMPLEX OF THE NI-FORM OF E.COLI DEFORMYLASE
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