3di0

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{{Seed}}
 
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[[Image:3di0.png|left|200px]]
 
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==Crystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureus==
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The line below this paragraph, containing "STRUCTURE_3di0", creates the "Structure Box" on the page.
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<StructureSection load='3di0' size='340' side='right'caption='[[3di0]], [[Resolution|resolution]] 2.38&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'>[[3di0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DI0 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]] 2.38&#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></td></tr>
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{{STRUCTURE_3di0| PDB=3di0 | 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=3di0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3di0 OCA], [https://pdbe.org/3di0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3di0 RCSB], [https://www.ebi.ac.uk/pdbsum/3di0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3di0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DAPA_STAAC DAPA_STAAC] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:18671976</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/di/3di0_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=3di0 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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Lysine biosynthesis is crucial for cell-wall formation in bacteria. Enzymes involved in lysine biosynthesis are thus potential targets for anti-microbial therapeutics. Dihydrodipicolinate synthase (DHDPS) catalyzes the first step of this pathway. Unlike its homologues, Staphylococcus aureus DHDPS is a dimer both in solution and in the crystal and is not feedback inhibited by lysine. The crystal structure of S. aureus DHDPS in the free and substrate bound forms provides a structural rationale for its catalytic mechanism. The structure also reveals unique conformational features of the S. aureus enzyme that could be crucial for the design of specific non-competitive inhibitors.
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===Crystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureus===
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Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase.,Girish TS, Sharma E, Gopal B FEBS Lett. 2008 Aug 20;582(19):2923-30. Epub 2008 Jul 29. PMID:18671976<ref>PMID:18671976</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 3di0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18671976}}, 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 18671976 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18671976}}
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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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3DI0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_col Staphylococcus aureus subsp. aureus col]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DI0 OCA].
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[[Category: Staphylococcus aureus subsp. aureus COL]]
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[[Category: Tavarekere GS]]
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==Reference==
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Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase., Girish TS, Sharma E, Gopal B, FEBS Lett. 2008 Aug 20;582(19):2923-30. Epub 2008 Jul 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18671976 18671976]
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[[Category: Dihydrodipicolinate synthase]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus subsp. aureus col]]
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[[Category: Tavarekere, G S.]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Cytoplasm]]
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[[Category: Diaminopimelate biosynthesis]]
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[[Category: Dihydrodipicolinate synthase]]
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[[Category: Feeb-back inhibition]]
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[[Category: Lyase]]
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[[Category: Lysine biosynthesis]]
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[[Category: Ping-pong mechanism]]
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[[Category: Schiff base]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 17 13:10:13 2008''
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Current revision

Crystal Structure of Dihydrodipicolinate synthase from Staphylococcus aureus

PDB ID 3di0

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