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[[Image:2yxg.gif|left|200px]]


{{Structure
==Crystal structure of Dihyrodipicolinate Synthase (dapA)==
|PDB= 2yxg |SIZE=350|CAPTION= <scene name='initialview01'>2yxg</scene>, resolution 2.20&Aring;
<StructureSection load='2yxg' size='340' side='right'caption='[[2yxg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY= [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]  
</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>
|GENE= dapA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
<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.


'''Crystal structure of Dihyrodipicolinate Synthase (dapA)'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yxg" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2YXG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXG OCA].
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
[[Category: Dihydrodipicolinate synthase]]
== References ==
[[Category: Methanocaldococcus jannaschii]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Bessho, Y.]]
</StructureSection>
[[Category: Padmanabhan, B.]]
[[Category: Large Structures]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Yokoyama, S.]]
[[Category: Bessho Y]]
[[Category: dihydrodipicolinate synthase]]
[[Category: Padmanabhan B]]
[[Category: lyase]]
[[Category: Yokoyama S]]
[[Category: mj0244]]
[[Category: national project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomic]]
[[Category: tim beta/alpha-barrel fold]]
 
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Retrieved from "https://proteopedia.org/2yxg"