1wa6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:29, 9 October 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1wa6.png|left|200px]]
 
-
<!--
+
==The structure of ACC oxidase==
-
The line below this paragraph, containing "STRUCTURE_1wa6", creates the "Structure Box" on the page.
+
<StructureSection load='1wa6' size='340' side='right'caption='[[1wa6]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1wa6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WA6 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_1wa6| PDB=1wa6 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wa6 OCA], [https://pdbe.org/1wa6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wa6 RCSB], [https://www.ebi.ac.uk/pdbsum/1wa6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wa6 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ACCO1_PETHY ACCO1_PETHY]
 +
== 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/wa/1wa6_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1wa6 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The final step in the biosynthesis of the plant signaling molecule ethylene is catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). ACCO requires bicarbonate as an activator and catalyzes the oxidation of ACC to give ethylene, CO2, and HCN. We report crystal structures of ACCO in apo-form (2.1 A resolution) and complexed with Fe(II) (2.55 A) or Co(II) (2.4 A). The active site contains a single Fe(II) ligated by three residues (His177, Asp179, and His234), and it is relatively open compared to those of the 2-oxoglutarate oxygenases. The side chains of Arg175 and Arg244, proposed to be involved in binding bicarbonate, project away from the active site, but conformational changes may allow either or both to enter the active site. The structures will form a basis for future mechanistic and inhibition studies.
-
===THE STRUCTURE OF ACC OXIDASE===
+
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme.,Zhang Z, Ren JS, Clifton IJ, Schofield CJ Chem Biol. 2004 Oct;11(10):1383-94. PMID:15489165<ref>PMID:15489165</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_15489165}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1wa6" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 15489165 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15489165}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1WA6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Petunia_x_hybrida Petunia x hybrida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA6 OCA].
+
-
 
+
-
==Reference==
+
-
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme., Zhang Z, Ren JS, Clifton IJ, Schofield CJ, Chem Biol. 2004 Oct;11(10):1383-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15489165 15489165]
+
-
[[Category: Aminocyclopropanecarboxylate oxidase]]
+
[[Category: Petunia x hybrida]]
[[Category: Petunia x hybrida]]
-
[[Category: Single protein]]
+
[[Category: Clifton IJ]]
-
[[Category: Clifton, I J.]]
+
[[Category: Ren J-S]]
-
[[Category: Ren, J S.]]
+
[[Category: Schofield CJ]]
-
[[Category: Schofield, C J.]]
+
[[Category: Zhang Z]]
-
[[Category: Zhang, Z.]]
+
-
[[Category: 2og oxygenase]]
+
-
[[Category: Acc oxidase]]
+
-
[[Category: Acco]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:53:45 2008''
+

Current revision

The structure of ACC oxidase

PDB ID 1wa6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools