3fqa: Difference between revisions

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-{{Seed}}
-[[Image:3fqa.png|left|200px]]
-<!--
+==Gabaculien complex of gabaculine resistant GSAM version==
-The line below this paragraph, containing "STRUCTURE_3fqa", creates the "Structure Box" on the page.
+<StructureSection load='3fqa' size='340' side='right'caption='[[3fqa]], [[Resolution|resolution]] 2.35&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'>[[3fqa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FQA 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]] 2.35&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAB:3-AMINOBENZOIC+ACID'>GAB</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr>
-{{STRUCTURE_3fqa|  PDB=3fqa  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fqa OCA], [https://pdbe.org/3fqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fqa RCSB], [https://www.ebi.ac.uk/pdbsum/3fqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fqa ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GSA_SYNP6 GSA_SYNP6]
+== 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/fq/3fqa_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=3fqa ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Gabaculine is a potent inhibitor of the vitamin B6-dependent key enzyme in chlorophyll biosynthesis, glutamate-1-semialdehyde aminomutase (GSAM). The inhibition effect is caused by an enzymatic deprotonation of the neurotoxin and requires the aldimine (PLP) form of the cofactor at the active site. In this study, we show that a single-point mutation confers resistance to gabaculine. A combined functional and structural analysis of wild-type GSAM in complex with gabaculine and the GSAM(M248I) form allowed us to decipher in atomic detail the molecular basis of this unique resistance. Interestingly, the gabaculine tolerance is caused by the absence of an essential water molecule that has a dual functional role. It serves as a nucleophilic shuttle for the hydroxyl anion along the reaction pathway and holds active-site Lys273 in a catalytically competent conformation. The single-point mutant is not able to fix this catalytic water between the beta-branched side chain of Ile248 and Lys273. As a consequence, the mutant enzyme is trapped in a gabaculine-insensitive but still enzymatically active amine (PMP) form.
-===Gabaculien complex of gabaculine resistant GSAM version===
+Absence of a catalytic water confers resistance to the neurotoxin gabaculine.,Orriss GL, Patel TR, Sorensen J, Stetefeld J FASEB J. 2010 Feb;24(2):404-14. Epub 2009 Sep 28. PMID:19786580<ref>PMID:19786580</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3fqa" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19786580}}, adds the Publication Abstract to the page
+*[[Aminomutase 3D structures|Aminomutase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19786580 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19786580}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-FQA is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_6301 Synechococcus elongatus pcc 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FQA OCA].
+[[Category: Synechococcus elongatus PCC 6301]]
+[[Category: Stetefeld J]]
-==Reference==
-<ref group="xtra">PMID:19786580</ref><references group="xtra"/>
-[[Category: Glutamate-1-semialdehyde 2,1-aminomutase]]
-[[Category: Synechococcus elongatus pcc 6301]]
-[[Category: Stetefeld, J.]]
-[[Category: Chlorophyll biosynthesis]]
-[[Category: Cytoplasm]]
-[[Category: Drug resistance]]
-[[Category: Integrated approach]]
-[[Category: Isomerase]]
-[[Category: Microevilution]]
-[[Category: Porphyrin biosynthesis]]
-[[Category: Pyridoxal phosphate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 28 14:52:55 2010''