3fce: Difference between revisions

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{{Seed}}
[[Image:3fce.png|left|200px]]


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==Crystal Structure of Bacillus cereus D-alanyl Carrier Protein Ligase DltA in Complex with ATP: Implications for Adenylation Mechanism==
The line below this paragraph, containing "STRUCTURE_3fce", creates the "Structure Box" on the page.
<StructureSection load='3fce' size='340' side='right'caption='[[3fce]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3fce]] 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=3FCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCE FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#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=CA:CALCIUM+ION'>CA</scene></td></tr>
{{STRUCTURE_3fce|  PDB=3fce  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fce OCA], [https://pdbe.org/3fce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fce RCSB], [https://www.ebi.ac.uk/pdbsum/3fce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fce ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/3fce_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3fce ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Crystal Structure of Bacillus cereus D-alanyl Carrier Protein Ligase DltA in Complex with ATP: Implications for Adenylation Mechanism===
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>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3fce" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 19324056 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19324056}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Bacillus cereus ATCC 14579]]
3FCE 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=3FCE OCA].
[[Category: Large Structures]]
 
[[Category: Du L]]
==Reference==
[[Category: He Y]]
<ref group="xtra">PMID:19324056</ref><references group="xtra"/>
[[Category: Luo Y]]
[[Category: Bacillus cereus atcc 14579]]
[[Category: Osman KT]]
[[Category: Du, L.]]
[[Category: He, Y.]]
[[Category: Luo, Y.]]
[[Category: Osman, K T.]]
[[Category: Adenylation]]
[[Category: Amp-forming domain]]
[[Category: Atp complex]]
[[Category: Cytoplasm]]
[[Category: D-alanine]]
[[Category: D-alanine carrier protein ligase]]
[[Category: Dlta]]
[[Category: Ligase]]
 
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Retrieved from "https://proteopedia.org/3fce"