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2yxg
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2yxg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2yxg, resolution 2.20Å" /> '''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" | ||
| - | caption="2yxg, resolution 2.20Å" /> | ||
| - | '''Crystal structure of Dihyrodipicolinate Synthase (dapA)'''<br /> | ||
| - | == | + | ==Crystal structure of Dihyrodipicolinate Synthase (dapA)== |
| - | + | <StructureSection load='2yxg' size='340' side='right'caption='[[2yxg]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [ | + | <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> |
| - | [ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=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> |
| - | [ | + | </table> |
| - | [ | + | == Function == |
| - | [ | + | [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] |
| - | [ | + | == Evolutionary Conservation == |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | [[ | + | Check<jmol> |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yxg_consurf.spt"</scriptWhenChecked> | |
| - | [ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[ | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | [ | + | </jmolCheckbox> |
| - | + | </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]. | |
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2yxg" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanocaldococcus jannaschii DSM 2661]] | ||
| + | [[Category: Bessho Y]] | ||
| + | [[Category: Padmanabhan B]] | ||
| + | [[Category: Yokoyama S]] | ||
Current revision
Crystal structure of Dihyrodipicolinate Synthase (dapA)
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