2bur: Difference between revisions
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==Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with 4-hydroxybenzoate== | |||
<StructureSection load='2bur' size='340' side='right' caption='[[2bur]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2bur' size='340' side='right' caption='[[2bur]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eo2|1eo2]], [[1eo9|1eo9]], [[1eoa|1eoa]], [[1eob|1eob]], [[1eoc|1eoc]], [[2bum|2bum]], [[2buq|2buq]], [[2but|2but]], [[2buu|2buu]], [[2buv|2buv]], [[2buw|2buw]], [[2bux|2bux]], [[2buy|2buy]], [[2buz|2buz]], [[2bv0|2bv0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eo2|1eo2]], [[1eo9|1eo9]], [[1eoa|1eoa]], [[1eob|1eob]], [[1eoc|1eoc]], [[2bum|2bum]], [[2buq|2buq]], [[2but|2but]], [[2buu|2buu]], [[2buv|2buv]], [[2buw|2buw]], [[2bux|2bux]], [[2buy|2buy]], [[2buz|2buz]], [[2bv0|2bv0]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] </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=2bur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bur OCA], [http://pdbe.org/2bur PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bur RCSB], [http://www.ebi.ac.uk/pdbsum/2bur 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=2bur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bur OCA], [http://pdbe.org/2bur PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bur RCSB], [http://www.ebi.ac.uk/pdbsum/2bur PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bur ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/2bur_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/2bur_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> | ||
Revision as of 09:44, 16 May 2018
Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with 4-hydroxybenzoateCrystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 in Complex with 4-hydroxybenzoate
Structural highlights
Function[PCXA_ACIAD] Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway. [PCXB_ACIAD] Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway. 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 PubMedThe catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase. Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.,Brown CK, Vetting MW, Earhart CA, Ohlendorf DH Annu Rev Microbiol. 2004;58:555-85. PMID:15487948[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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