1eb4

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[[Image:1eb4.jpg|left|200px]]<br /><applet load="1eb4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eb4, resolution 2.0&Aring;" />
 
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'''HISTIDINE AMMONIA-LYASE (HAL) MUTANT F329A FROM PSEUDOMONAS PUTIDA'''<br />
 
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==Overview==
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==Histidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida==
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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.
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<StructureSection load='1eb4' size='340' side='right'caption='[[1eb4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eb4]] is a 1 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=1EB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB4 FirstGlance]. <br>
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</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&#8491;</td></tr>
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<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=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb4 OCA], [https://pdbe.org/1eb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eb4 RCSB], [https://www.ebi.ac.uk/pdbsum/1eb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eb4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HUTH_PSEPU HUTH_PSEPU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/1eb4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1eb4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1EB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Histidine_ammonia-lyase Histidine ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.3 4.3.1.3] Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EB4 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase., Baedeker M, Schulz GE, Structure. 2002 Jan;10(1):61-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11796111 11796111]
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</div>
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[[Category: Histidine ammonia-lyase]]
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<div class="pdbe-citations 1eb4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Baedeker M]]
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[[Category: Baedeker, M.]]
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[[Category: Schulz GE]]
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[[Category: Schulz, G.E.]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: ammonia-lyase]]
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[[Category: histidine degradation]]
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[[Category: lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:09:05 2007''
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Current revision

Histidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida

PDB ID 1eb4

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