3fcc

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{{Seed}}
 
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[[Image:3fcc.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF DLTA PROTEIN IN COMPLEX WITH ATP and MAGNESIUM==
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The line below this paragraph, containing "STRUCTURE_3fcc", creates the "Structure Box" on the page.
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<StructureSection load='3fcc' size='340' side='right'caption='[[3fcc]], [[Resolution|resolution]] 2.32&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'>[[3fcc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCC 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]] 2.32&#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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_3fcc| PDB=3fcc | 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=3fcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcc OCA], [https://pdbe.org/3fcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcc RCSB], [https://www.ebi.ac.uk/pdbsum/3fcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DLTA_BACCR DLTA_BACCR] Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Catalyzes an ATP-dependent two-step reaction where it forms a high energy D-alanyl AMP intermediate and transfers the alanyl residues from AMP to Dcp (By similarity).
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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/fc/3fcc_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=3fcc 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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D-alanylation of lipoteichoic acids modulates the surface charge and ligand binding of the Gram-positive cell wall. Disruption of the bacterial dlt operon involved in teichoic acid alanylation, as well as inhibition of the DltA (D-alanyl carrier protein ligase) protein, has been shown to render the bacterium more susceptible to conventional antibiotics and host defense responses. The DltA catalyzes the adenylation and thiolation reactions of d-alanine. This enzyme belongs to a superfamily of AMP-forming domains such as the ubiquitous acetyl-coenzyme A synthetase. We have determined the 1.9-A-resolution crystal structure of a DltA protein from Bacillus cereus in complex with ATP. This structure sheds light on the geometry of the bound ATP. The invariant catalytic residue Lys492 appears to be mobile, suggesting a molecular mechanism of catalysis for this superfamily of enzymes. Specific roles are also revealed for two other invariant residues: the divalent cation-stabilizing Glu298 and the beta-phosphate-interacting Arg397. Mutant proteins with a glutamine substitution at position 298 or 397 are inactive.
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===CRYSTAL STRUCTURE OF DLTA PROTEIN IN COMPLEX WITH ATP and MAGNESIUM===
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Crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) in complex with ATP.,Osman KT, Du L, He Y, Luo Y J Mol Biol. 2009 May 1;388(2):345-55. Epub 2009 Mar 24. PMID:19324056<ref>PMID:19324056</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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The line below this paragraph, {{ABSTRACT_PUBMED_19324056}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3fcc" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19324056 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19324056}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Bacillus cereus ATCC 14579]]
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3FCC is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_atcc_14579 Bacillus cereus atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FCC OCA].
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[[Category: Large Structures]]
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[[Category: Du L]]
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==Reference==
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[[Category: He Y]]
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<ref group="xtra">PMID:19324056</ref><references group="xtra"/>
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[[Category: Luo Y]]
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[[Category: Bacillus cereus atcc 14579]]
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[[Category: Osman KT]]
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[[Category: Du, L.]]
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[[Category: He, Y.]]
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[[Category: Luo, Y.]]
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[[Category: Osman, K T.]]
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[[Category: Adenylation]]
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[[Category: Amp-forming domain]]
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[[Category: Atp complex]]
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[[Category: Cytoplasm]]
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[[Category: D-alanine]]
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[[Category: D-alanine carrier protein ligase]]
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[[Category: Dlta]]
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[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 6 10:11:33 2009''
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Current revision

CRYSTAL STRUCTURE OF DLTA PROTEIN IN COMPLEX WITH ATP and MAGNESIUM

PDB ID 3fcc

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