2bur: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bur]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BUR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2bur]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BUR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene></td></tr> | ||
<tr><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><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><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://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://www.rcsb.org/pdb/explore.do?structureId=2bur RCSB], [http://www.ebi.ac.uk/pdbsum/2bur PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 35: | ||
[[Category: Acinetobacter calcoaceticus]] | [[Category: Acinetobacter calcoaceticus]] | ||
[[Category: Protocatechuate 3,4-dioxygenase]] | [[Category: Protocatechuate 3,4-dioxygenase]] | ||
[[Category: Argenio, D A.D | [[Category: Argenio, D A.D]] | ||
[[Category: Lipscomb, J D | [[Category: Lipscomb, J D]] | ||
[[Category: Ohlendorf, D H | [[Category: Ohlendorf, D H]] | ||
[[Category: Ornston, L N | [[Category: Ornston, L N]] | ||
[[Category: Valley, M P | [[Category: Valley, M P]] | ||
[[Category: Vetting, M W | [[Category: Vetting, M W]] | ||
[[Category: Aromatic degradation]] | [[Category: Aromatic degradation]] | ||
[[Category: Beta- sandwich]] | [[Category: Beta- sandwich]] | ||
Revision as of 21:20, 15 January 2015
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
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
|
| ||||||||||||||||||||