1gk2
From Proteopedia
(Difference between revisions)
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<StructureSection load='1gk2' size='340' side='right'caption='[[1gk2]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1gk2' size='340' side='right'caption='[[1gk2]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1gk2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1gk2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GK2 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1gk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk2 OCA], [https://pdbe.org/1gk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gk2 RCSB], [https://www.ebi.ac.uk/pdbsum/1gk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk2 ProSAT]</span></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=1gk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk2 OCA], [https://pdbe.org/1gk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gk2 RCSB], [https://www.ebi.ac.uk/pdbsum/1gk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HUTH_PSEPU HUTH_PSEPU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1gk2 ConSurf]. | </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=1gk2 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Histidine ammonia-lyase requires a 4-methylidene-imidazole-5-one group (MIO) that is produced autocatalytically by a cyclization and dehydration step in a 3-residue loop of the polypeptide. The crystal structures of three mutants have been established. Two mutants were inactive and failed to form MIO, but remained unchanged elsewhere. The third mutant showed very low activity and formed MIO, although it differed from an MIO-less mutant only by an additional 329-C(beta) atom. This atom forms one constraint during MIO formation, the other being the strongly connected Asp145. An exploration of the conformational space of the MIO-forming loop showed that the cyclization is probably enforced by a mechanic compression in a late stage of chain folding and is catalyzed by a well-connected internal water molecule. The cyclization of the respective 3-residue loop of green fluorescent protein is likely to occur in a similar reaction. | ||
- | |||
- | Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase.,Baedeker M, Schulz GE Structure. 2002 Jan;10(1):61-7. PMID:11796111<ref>PMID:11796111</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1gk2" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Bacillus fluorescens putidus flugge 1886]] | ||
- | [[Category: Histidine ammonia-lyase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Pseudomonas putida]] |
- | [[Category: | + | [[Category: Baedeker M]] |
- | [[Category: | + | [[Category: Schulz GE]] |
- | + |
Revision as of 11:21, 27 March 2024
Histidine Ammonia-Lyase (HAL) Mutant F329G from Pseudomonas putida
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