1gpw
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:1gpw.png|left|200px]] | ||
- | < | + | ==Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex.== |
- | + | <StructureSection load='1gpw' size='340' side='right'caption='[[1gpw]], [[Resolution|resolution]] 2.40Å' scene=''> | |
- | You may | + | == Structural highlights == |
- | + | <table><tr><td colspan='2'>[[1gpw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GPW 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]] 2.4Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1gpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpw OCA], [https://pdbe.org/1gpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gpw RCSB], [https://www.ebi.ac.uk/pdbsum/1gpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gpw ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HIS6_THEMA HIS6_THEMA] IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013] | ||
+ | == 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/gp/1gpw_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=1gpw ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Since reactive ammonia is not available under physiological conditions, glutamine is used as a source for the incorporation of nitrogen in a number of metabolic pathway intermediates. The heterodimeric ImGP synthase that links histidine and purine biosynthesis belongs to the family of glutamine amidotransferases in which the glutaminase activity is coupled with a subsequent synthase activity specific for each member of the enzyme family. Its X-ray structure from the hyperthermophile Thermotoga maritima shows that the glutaminase subunit is associated with the N-terminal face of the (beta alpha)(8) barrel cyclase subunit. The complex reveals a putative tunnel for the transfer of ammonia over a distance of 25 A. Although ammonia tunneling has been reported for glutamine amidotransferases, the ImGP synthase has evolved a novel mechanism, which extends the known functional properties of the versatile (beta alpha)(8) barrel fold. | ||
- | + | Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex.,Douangamath A, Walker M, Beismann-Driemeyer S, Vega-Fernandez MC, Sterner R, Wilmanns M Structure. 2002 Feb;10(2):185-93. PMID:11839304<ref>PMID:11839304</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1gpw" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Large Structures]] |
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- | == | + | |
- | < | + | |
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
- | [[Category: Beismann-Driemeyer | + | [[Category: Beismann-Driemeyer S]] |
- | [[Category: Sterner | + | [[Category: Sterner R]] |
- | [[Category: Walker | + | [[Category: Walker M]] |
- | [[Category: Wilmanns | + | [[Category: Wilmanns M]] |
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Current revision
Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex.
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