3flu

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{{Seed}}
 
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[[Image:3flu.jpg|left|200px]]
 
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==Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis==
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The line below this paragraph, containing "STRUCTURE_3flu", creates the "Structure Box" on the page.
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<StructureSection load='3flu' size='340' side='right'caption='[[3flu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3flu]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3FLU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_3flu| PDB=3flu | SCENE= }}
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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=3flu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3flu OCA], [https://pdbe.org/3flu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3flu RCSB], [https://www.ebi.ac.uk/pdbsum/3flu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3flu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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/main_output.php?pdb_ID=3flu 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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===Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis===
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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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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 3flu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19236959}}, adds the Publication Abstract to the page
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*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19236959 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19236959}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3FLU is a 4 chains structure of sequences 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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[[Category: Neisseria meningitidis serogroup B]]
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[[Category: Devenish SRA]]
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==Reference==
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[[Category: Hadfield AT]]
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<ref group="xtra">PMID:19236959</ref><references group="xtra"/>
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[[Category: Dihydrodipicolinate synthase]]
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[[Category: Neisseria meningitidis serogroup b]]
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[[Category: Devenish, S R.A.]]
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[[Category: Hadfield, A T.]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Beta-alpha-barrel]]
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[[Category: Cytoplasm]]
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[[Category: Diaminopimelate biosynthesis]]
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[[Category: Lyase]]
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[[Category: Lysine biosynthesis]]
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[[Category: Schiff base]]
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[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 25 09:10:02 2009''
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Current revision

Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis

PDB ID 3flu

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