1iax

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1iax" [edit=sysop:move=sysop])
Current revision (22:03, 26 March 2025) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1iax.png|left|200px]]
 
-
{{STRUCTURE_1iax| PDB=1iax | SCENE= }}
+
==CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH PLP==
 +
<StructureSection load='1iax' size='340' side='right'caption='[[1iax]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1iax]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAX 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]] 2.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1iax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iax OCA], [https://pdbe.org/1iax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iax RCSB], [https://www.ebi.ac.uk/pdbsum/1iax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iax ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/1A12_SOLLC 1A12_SOLLC] 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.
 +
== 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/ia/1iax_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=1iax ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS) in complex with either cofactor pyridoxal-5'-phosphate (PLP) or both PLP and inhibitor aminoethoxyvinylglycine have been determined by x-ray crystallography. The structures showed good conservation of the catalytic residues, suggesting a similar catalytic mechanism for ACS and other PLP-dependent enzymes. However, the proximity of Tyr152 to the C-gamma-S bond of model substrate S-adenosylmethionine implies its critical role in the catalysis. The concerted accomplishment of catalysis by cofactor PLP and a protein residue, as proposed on the basis of the ACS structures in this paper, may represent a general scheme for the diversity of PLP-dependent catalyses. PLP-dependent enzymes have been categorized into four types of folds. A structural comparison revealed that a core fragment of ACS in fold type I is superimposable over tryptophan synthase beta subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes.
-
===CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH PLP===
+
Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms.,Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H J Biol Chem. 2001 Oct 12;276(41):38210-6. Epub 2001 Jun 28. PMID:11431475<ref>PMID:11431475</ref>
-
{{ABSTRACT_PUBMED_11431475}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1iax" style="background-color:#fffaf0;"></div>
-
[[1iax]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAX OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:011431475</ref><references group="xtra"/>
+
</StructureSection>
-
[[Category: 1-aminocyclopropane-1-carboxylate synthase]]
+
[[Category: Large Structures]]
[[Category: Solanum lycopersicum]]
[[Category: Solanum lycopersicum]]
-
[[Category: Callahan, B.]]
+
[[Category: Callahan B]]
-
[[Category: Chen, Y.]]
+
[[Category: Chen Y]]
-
[[Category: Huai, Q.]]
+
[[Category: Huai Q]]
-
[[Category: Ke, H.]]
+
[[Category: Ke H]]
-
[[Category: Li, N.]]
+
[[Category: Li N]]
-
[[Category: Xia, Y.]]
+
[[Category: Xia Y]]
-
[[Category: Lyase]]
+
-
[[Category: Plp-dependent enzyme]]
+

Current revision

CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH PLP

PDB ID 1iax

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/1iax"
Personal tools