1kwc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==The His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenyl== | ==The His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenyl== | ||
<StructureSection load='1kwc' size='340' side='right' caption='[[1kwc]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1kwc' size='340' side='right' caption='[[1kwc]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| Line 6: | Line 7: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kw3|1kw3]], [[1kw6|1kw6]], [[1kw8|1kw8]], [[1kw9|1kw9]], [[1kwb|1kwb]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kw3|1kw3]], [[1kw6|1kw6]], [[1kw8|1kw8]], [[1kw9|1kw9]], [[1kwb|1kwb]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Biphenyl-2,3-diol_1,2-dioxygenase Biphenyl-2,3-diol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.39 1.13.11.39] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Biphenyl-2,3-diol_1,2-dioxygenase Biphenyl-2,3-diol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.39 1.13.11.39] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwc OCA], [http://pdbe.org/1kwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kwc RCSB], [http://www.ebi.ac.uk/pdbsum/1kwc PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kwc OCA], [http://pdbe.org/1kwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kwc RCSB], [http://www.ebi.ac.uk/pdbsum/1kwc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kwc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 12: | Line 13: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/1kwc_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kw/1kwc_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 27: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1kwc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1kwc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 00:35, 25 January 2018
The His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenylThe His145Ala mutant of 2,3-dihydroxybiphenyl dioxygenase in complex with 2,3-dihydroxybiphenyl
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBphC derived from Pseudomonas sp. strain KKS102 is an extradiol-cleaving catecholic dioxygenase. This enzyme contains a non-heme iron atom and plays an important role in degrading biphenyl/polychlorinated biphenyls (PCBs) in the microbe. To elucidate detailed structures of BphC reaction intermediates, crystal structures of the substrate-free form, the BphC-substrate complex, and the BphC-substrate-NO (nitric oxide) complex were determined. These crystal structures revealed (1) the binding site of the O(2) molecule in the coordination sphere and (2) conformational changes of His194 during the catalytic reaction. On the basis of these findings, we propose a catalytic mechanism for the extradiol-cleaving catecholic dioxygenase in which His194 seems to play three distinct roles. At the early stage of the catalytic reaction, His194 appears to act as a catalytic base, which likely deprotonates the hydroxyl group of the substrate. At the next stage, the protonated His194 seems to stabilize a negative charge on the O2 molecule located in the hydrophobic O2-binding cavity. Finally, protonated His194 seems to function as a proton donor, whose existence has been proposed. Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase.,Sato N, Uragami Y, Nishizaki T, Takahashi Y, Sazaki G, Sugimoto K, Nonaka T, Masai E, Fukuda M, Senda T J Mol Biol. 2002 Aug 23;321(4):621-36. PMID:12206778[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||||||