11as

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(New page: 200px<br /><applet load="11as" size="450" color="white" frame="true" align="right" spinBox="true" caption="11as, resolution 2.5&Aring;" /> '''ASPARAGINE SYNTHETASE...)
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[[Image:11as.jpg|left|200px]]<br /><applet load="11as" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="11as, resolution 2.5&Aring;" />
 
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'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''<br />
 
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==Overview==
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==ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE==
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The crystal structure of E. coli asparagine synthetase has been determined, by X-ray diffraction analysis at 2.5 A resolution. The overall structure, of the enzyme is remarkably similar to that of the catalytic domain of, yeast aspartyl-tRNA synthetase despite low sequence similarity. These, enzymes have a common reaction mechanism that implies the formation of an, aminoacyl-adenylate intermediate. The active site architecture and most of, the catalytic residues are also conserved in both enzymes. These proteins, have probably evolved from a common ancestor even though their sequence, similarities are small. The functional and structural similarities of both, enzymes suggest that new enzymatic activities would generally follow the, recruitment of a protein catalyzing a similar chemical reaction.
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<StructureSection load='11as' size='340' side='right'caption='[[11as]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[11as]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=11AS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=11AS 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]] 2.5&#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=ASN:ASPARAGINE'>ASN</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=11as FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11as OCA], [https://pdbe.org/11as PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=11as RCSB], [https://www.ebi.ac.uk/pdbsum/11as PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=11as ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASNA_ECOLI ASNA_ECOLI] May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn (Probable).<ref>PMID:17962566</ref>
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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/1a/11as_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=11as ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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11AS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ASN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate--ammonia_ligase Aspartate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.1 6.3.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=11AS OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase., Nakatsu T, Kato H, Oda J, Nat Struct Biol. 1998 Jan;5(1):15-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9437423 9437423]
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__TOC__
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[[Category: Aspartate--ammonia ligase]]
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kato, H.]]
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[[Category: Kato H]]
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[[Category: Nakatsu, T.]]
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[[Category: Nakatsu T]]
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[[Category: Oda, J.]]
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[[Category: Oda J]]
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[[Category: ASN]]
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[[Category: asparagine synthetase]]
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[[Category: ligase]]
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[[Category: nitrogen fixation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:25:41 2007''
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Current revision

ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE

PDB ID 11as

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