3flu

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[[Image:3flu.png|left|200px]]
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==Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis==
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<StructureSection load='3flu' size='340' side='right' caption='[[3flu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3flu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_b Neisseria meningitidis serogroup b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FLU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yxc|1yxc]], [[1yxd|1yxd]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA, NMB0929 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 Neisseria meningitidis serogroup B])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3flu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3flu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3flu RCSB], [http://www.ebi.ac.uk/pdbsum/3flu PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DAPA_NEIMB DAPA_NEIMB]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:19236959</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/fl/3flu_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/chain_selection.php?pdb_ID=2ata 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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Neisseria meningitidis is an obligate commensal bacterium of humans, and also an important human pathogen. To facilitate future drug studies, we report here the biochemical and structural characterisation of a key enzyme in (S)-lysine biosynthesis, dihydrodipicolinate synthase (DHDPS), from N. meningitidis (NmeDHDPS). X-ray crystallography revealed only minor structural differences between NmeDHDPS and the enzyme from E. coli at the active and allosteric effector sites. The catalytic capabilities of NmeDHDPS are similar to those of the enzyme from E. coli, but intriguingly NmeDHDPS is subject to substrate inhibition by high concentrations of the second substrate, (S)-aspartate semialdehyde, and is also significantly more sensitive to feedback inhibition by (S)-lysine. This heightened sensitivity to inhibition at both active and allosteric sites suggests that it may be possible to target DHDPS from N. meningitidis for antibiotic development.
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{{STRUCTURE_3flu| PDB=3flu | SCENE= }}
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Cloning and characterisation of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis.,Devenish SR, Huisman FH, Parker EJ, Hadfield AT, Gerrard JA Biochim Biophys Acta. 2009 Aug;1794(8):1168-74. Epub 2009 Feb 21. PMID:19236959<ref>PMID:19236959</ref>
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===Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis===
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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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{{ABSTRACT_PUBMED_19236959}}
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==About this Structure==
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[[3flu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_b Neisseria meningitidis serogroup b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FLU OCA].
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==See Also==
==See Also==
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*[[Dihydrodipicolinate Synthase|Dihydrodipicolinate Synthase]]
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019236959</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Dihydrodipicolinate synthase]]
[[Category: Dihydrodipicolinate synthase]]
[[Category: Neisseria meningitidis serogroup b]]
[[Category: Neisseria meningitidis serogroup b]]
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[[Category: Devenish, S R.A.]]
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[[Category: Devenish, S R.A]]
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[[Category: Hadfield, A T.]]
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[[Category: Hadfield, A T]]
[[Category: Amino-acid biosynthesis]]
[[Category: Amino-acid biosynthesis]]
[[Category: Beta-alpha-barrel]]
[[Category: Beta-alpha-barrel]]

Revision as of 12:54, 5 January 2015

Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis

3flu, resolution 2.00Å

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