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1gqz

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[[Image:1gqz.gif|left|200px]]
 
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{{Structure
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==Refinement of Haemophilus influenzae Diaminopimelate epimerase at 1.7A==
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|PDB= 1gqz |SIZE=350|CAPTION= <scene name='initialview01'>1gqz</scene>, resolution 1.75&Aring;
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<StructureSection load='1gqz' size='340' side='right'caption='[[1gqz]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1gqz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GQZ FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Diaminopimelate_epimerase Diaminopimelate epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.7 5.1.1.7] </span>
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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]] 1.75&#8491;</td></tr>
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|GENE=
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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=1gqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqz OCA], [https://pdbe.org/1gqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gqz RCSB], [https://www.ebi.ac.uk/pdbsum/1gqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gqz ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqz OCA], [http://www.ebi.ac.uk/pdbsum/1gqz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gqz RCSB]</span>
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[https://www.uniprot.org/uniprot/DAPF_HAEIN DAPF_HAEIN] Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Only accepts DAP isomers with the L configuration.<ref>PMID:10194362</ref>
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}}
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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/gq/1gqz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1gqz 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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Diaminopimelate (DAP) epimerase (DapF) is central to the biosynthesis of both lysine and cell-wall peptidoglycan in many bacteria species. The peptidoglycan layer provides great potential for the development of novel antimicrobials as it is a uniquely prokaryotic feature. Crystals of recombinant Haemophilus influenzae DapF that diffract to beyond 2 A resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 A higher than that previously determined. An analysis of the structure (i) in comparison to other PLP-independent racemaces and (ii) in relation to the catalytic mechanism and stereospecificity of DapF is presented.
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'''REFINEMENT OF HAEMOPHILUS INFLUENZAE DIAMINOPIMELATE EPIMERASE AT 1.7A'''
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Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis.,Lloyd AJ, Huyton T, Turkenburg J, Roper DI Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):397-400. Epub 2004, Jan 23. PMID:14747737<ref>PMID:14747737</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==About this Structure==
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</div>
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1GQZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQZ OCA].
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<div class="pdbe-citations 1gqz" style="background-color:#fffaf0;"></div>
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[[Category: Diaminopimelate epimerase]]
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== References ==
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[[Category: Haemophilus influenzae]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Huyton, T.]]
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</StructureSection>
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[[Category: Roper, D I.]]
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[[Category: Haemophilus influenzae Rd KW20]]
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[[Category: Turkenburg, J P.]]
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[[Category: Large Structures]]
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[[Category: isomerase]]
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[[Category: Huyton T]]
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[[Category: peptidoglycan biosynthesis]]
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[[Category: Roper DI]]
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[[Category: Turkenburg JP]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:49:38 2008''
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Current revision

Refinement of Haemophilus influenzae Diaminopimelate epimerase at 1.7A

PDB ID 1gqz

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