2bum

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:55, 13 December 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_2bum| PDB=2bum | SCENE= }}
 
-
===CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1===
 
-
{{ABSTRACT_PUBMED_15487948}}
 
-
==About this Structure==
+
==Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1==
-
[[2bum]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_sp. Acinetobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUM OCA].
+
<StructureSection load='2bum' size='340' side='right'caption='[[2bum]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2bum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi_ADP1 Acinetobacter baylyi ADP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUM FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 +
<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=OH:HYDROXIDE+ION'>OH</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=2bum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bum OCA], [https://pdbe.org/2bum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bum RCSB], [https://www.ebi.ac.uk/pdbsum/2bum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bum ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PCXA_ACIAD PCXA_ACIAD] Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
 +
== 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/bu/2bum_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/main_output.php?pdb_ID=2bum ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The 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.
-
==See Also==
+
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<ref>PMID:15487948</ref>
-
*[[Dioxygenase|Dioxygenase]]
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:015487948</ref><references group="xtra"/><references/>
+
</div>
-
[[Category: Acinetobacter sp.]]
+
<div class="pdbe-citations 2bum" style="background-color:#fffaf0;"></div>
-
[[Category: Protocatechuate 3,4-dioxygenase]]
+
 
-
[[Category: Argenio, D A.D.]]
+
==See Also==
-
[[Category: Lipscomb, J D.]]
+
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
-
[[Category: Ohlendorf, D H.]]
+
== References ==
-
[[Category: Ornston, L N.]]
+
<references/>
-
[[Category: Valley, M P.]]
+
__TOC__
-
[[Category: Vetting, M W.]]
+
</StructureSection>
-
[[Category: Aromatic degradation]]
+
[[Category: Acinetobacter baylyi ADP1]]
-
[[Category: Beta-sandwich]]
+
[[Category: Large Structures]]
-
[[Category: Mixed alpha/beta structure]]
+
[[Category: D'Argenio DA]]
-
[[Category: Non-heme iron]]
+
[[Category: Lipscomb JD]]
-
[[Category: Oxidoreductase]]
+
[[Category: Ohlendorf DH]]
 +
[[Category: Ornston LN]]
 +
[[Category: Valley MP]]
 +
[[Category: Vetting MW]]

Current revision

Crystal Structure Of Wild-Type Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1

PDB ID 2bum

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bum"
Personal tools