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1dhp

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[[Image:1dhp.gif|left|200px]]
 
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{{Structure
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==DIHYDRODIPICOLINATE SYNTHASE==
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|PDB= 1dhp |SIZE=350|CAPTION= <scene name='initialview01'>1dhp</scene>, resolution 2.3&Aring;
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<StructureSection load='1dhp' size='340' side='right'caption='[[1dhp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE= <scene name='pdbsite=S1:Pyruvate+Binding+Residue'>S1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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<table><tr><td colspan='2'>[[1dhp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DHP FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </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]] 2.3&#8491;</td></tr>
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|GENE= DAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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|DOMAIN=
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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=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [https://pdbe.org/1dhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB], [https://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dhp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dhp OCA], [http://www.ebi.ac.uk/pdbsum/1dhp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dhp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</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/dh/1dhp_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=1dhp ConSurf].
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<div style="clear:both"></div>
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'''DIHYDRODIPICOLINATE SYNTHASE'''
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==See Also==
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
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== References ==
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==Overview==
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<references/>
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The crystal structure of dihydrodipicolinate synthase from E. coli was determined by multiple isomorphous replacement methods. The structure was refined at a resolution of 2.5 A and the final R-factor is 19.6% for 32,190 reflections between 10.0 A and 2.5 A and F &gt; 2 sigma (F). The crystallographic asymmetric unit contains two monomers related by approximate 2-fold symmetry. A tetramer with approximate 222 symmetry is built up by crystallographic symmetry. The tetramer is almost planar with no contacts between the subunits related by the non-crystallographic dyad. The active sites are accessible from a wide water-filled channel in the center of the tetramer. The dihydrodipicolinate synthase monomer is composed of two domains. Each polypeptide chain is folded into an 8-fold alpha/beta barrel and a C-terminal alpha-helical domain comprising residues 224 to 292. The fold is similar to that of N-acetylneuraminate lyase. The active site lysine 161 is located in the alpha/beta barrel and has access via two entrances from the C-terminal side of the barrel.
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__TOC__
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</StructureSection>
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==About this Structure==
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1DHP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHP OCA].
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==Reference==
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The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution., Mirwaldt C, Korndorfer I, Huber R, J Mol Biol. 1995 Feb 10;246(1):227-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7853400 7853400]
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[[Category: Dihydrodipicolinate synthase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Korndoerfer, I.]]
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[[Category: Korndoerfer I]]
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[[Category: Mirwaldt, C.]]
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[[Category: Mirwaldt C]]
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[[Category: dihydrodipicolinate]]
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[[Category: synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:45 2008''
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Current revision

DIHYDRODIPICOLINATE SYNTHASE

PDB ID 1dhp

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