2yxg

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(New page: 200px<br /><applet load="2yxg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2yxg, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:2yxg.gif|left|200px]]<br /><applet load="2yxg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2yxg, resolution 2.20&Aring;" />
 
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'''Crystal structure of Dihyrodipicolinate Synthase (dapA)'''<br />
 
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==About this Structure==
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==Crystal structure of Dihyrodipicolinate Synthase (dapA)==
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2YXG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Active as [http://en.wikipedia.org/wiki/Dihydrodipicolinate_synthase Dihydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.52 4.2.1.52] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXG OCA].
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<StructureSection load='2yxg' size='340' side='right'caption='[[2yxg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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[[Category: Dihydrodipicolinate synthase]]
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== Structural highlights ==
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[[Category: Methanocaldococcus jannaschii]]
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<table><tr><td colspan='2'>[[2yxg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YXG FirstGlance]. <br>
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[[Category: Single protein]]
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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]] 2.2&#8491;</td></tr>
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[[Category: Bessho, Y.]]
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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=2yxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yxg OCA], [https://pdbe.org/2yxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yxg RCSB], [https://www.ebi.ac.uk/pdbsum/2yxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yxg ProSAT], [https://www.topsan.org/Proteins/RSGI/2yxg TOPSAN]</span></td></tr>
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[[Category: Padmanabhan, B.]]
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</table>
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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== Function ==
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[[Category: Yokoyama, S.]]
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[https://www.uniprot.org/uniprot/DAPA_METJA DAPA_METJA] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418]
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[[Category: dihydrodipicolinate synthase]]
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== Evolutionary Conservation ==
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[[Category: lyase]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: mj0244]]
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Check<jmol>
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[[Category: national project on protein structural and functional analyses]]
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<jmolCheckbox>
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[[Category: nppsfa]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yxg_consurf.spt"</scriptWhenChecked>
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[[Category: riken structural genomics/proteomics initiative]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: rsgi]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: structural genomics]]
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</jmolCheckbox>
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[[Category: tim beta/alpha-barrel fold]]
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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=2yxg 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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In bacteria and plants, dihydrodipicolinate synthase (DHDPS) plays a key role in the (S)-lysine biosynthesis pathway. DHDPS catalyzes the first step of the condensation of (S)-aspartate-beta-semialdehyde and pyruvate to form an unstable compound, (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid. The activity of DHDPS is allosterically regulated by (S)-lysine, a feedback inhibitor. The crystal structure of DHDPS from Methanocaldococcus jannaschii (MjDHDPS) was solved by the molecular-replacement method and was refined to 2.2 A resolution. The structure revealed that MjDHDPS forms a functional homotetramer, as also observed in Escherichia coli DHDPS, Thermotoga maritima DHDPS and Bacillus anthracis DHDPS. The binding-site region of MjDHDPS is essentially similar to those found in other known DHDPS structures.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:39:25 2008''
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Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.,Padmanabhan B, Strange RW, Antonyuk SV, Ellis MJ, Hasnain SS, Iino H, Agari Y, Bessho Y, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1222-6. Epub 2009 Nov 27. PMID:20054116<ref>PMID:20054116</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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</div>
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<div class="pdbe-citations 2yxg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
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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]]
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[[Category: Methanocaldococcus jannaschii DSM 2661]]
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[[Category: Bessho Y]]
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[[Category: Padmanabhan B]]
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[[Category: Yokoyama S]]

Current revision

Crystal structure of Dihyrodipicolinate Synthase (dapA)

PDB ID 2yxg

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