This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2but

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:56, 13 December 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2but.png|left|200px]]
 
-
{{STRUCTURE_2but| PDB=2but | SCENE= }}
+
==Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S - APO==
 +
<StructureSection load='2but' size='340' side='right'caption='[[2but]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2but]] 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=2BUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUT 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]] 1.85&#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=2but FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2but OCA], [https://pdbe.org/2but PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2but RCSB], [https://www.ebi.ac.uk/pdbsum/2but PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2but 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/2but_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=2but 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.
-
===CRYSTAL STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 MUTANT R457S - APO===
+
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>
-
{{ABSTRACT_PUBMED_15487948}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2but" style="background-color:#fffaf0;"></div>
-
==About this Structure==
+
==See Also==
-
[[2but]] 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=2BUT OCA].
+
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:015487948</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Acinetobacter calcoaceticus]]
+
</StructureSection>
-
[[Category: Protocatechuate 3,4-dioxygenase]]
+
[[Category: Acinetobacter baylyi ADP1]]
-
[[Category: Argenio, D A.D.]]
+
[[Category: Large Structures]]
-
[[Category: Lipscomb, J D.]]
+
[[Category: D'Argenio DA]]
-
[[Category: Ohlendorf, D H.]]
+
[[Category: Lipscomb JD]]
-
[[Category: Ornston, L N.]]
+
[[Category: Ohlendorf DH]]
-
[[Category: Valley, M P.]]
+
[[Category: Ornston LN]]
-
[[Category: Vetting, M W.]]
+
[[Category: Valley MP]]
-
[[Category: Aromatic degradation]]
+
[[Category: Vetting MW]]
-
[[Category: Aromatic hydrocarbons catabolism]]
+
-
[[Category: Dioxygenase]]
+
-
[[Category: Iron]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Non-heme iron]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S - APO

PDB ID 2but

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools