2l0r

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[[Image:2l0r.png|left|200px]]
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==Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center==
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<StructureSection load='2l0r' size='340' side='right' caption='[[2l0r]], [[NMR_Ensembles_of_Models | 31 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2l0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L0R FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BXA0172, GBAA_pXO1_0172, lef, pXO1-107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])</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/Anthrax_lethal_factor_endopeptidase Anthrax lethal factor endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.83 3.4.24.83] </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=2l0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l0r RCSB], [http://www.ebi.ac.uk/pdbsum/2l0r PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Anthrax lethal factor (LF) is a zinc-metalloprotease that together with the protective antigen constitutes anthrax lethal toxin, which is the most prominent virulence factor of the anthrax disease. The solution nuclear magnetic resonance and in silico conformational dynamics of the 105 C-terminal residues of the LF catalytic core domain in its apo form are described here. The polypeptide adopts a compact structure even in the absence of the Zn(2+) cofactor, while the 40 N-terminal residues comprising the metal ligands and residues that participate in substrate and inhibitor recognition exhibit more flexibility than the C-terminal region.
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{{STRUCTURE_2l0r| PDB=2l0r | SCENE= }}
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Conformational dynamics of the anthrax lethal factor catalytic center.,Dalkas GA, Chasapis CT, Gkazonis PV, Bentrop D, Spyroulias GA Biochemistry. 2010 Dec 28;49(51):10767-9. Epub 2010 Dec 3. PMID:21121613<ref>PMID:21121613</ref>
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===Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center===
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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_21121613}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2l0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0R OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:021121613</ref><references group="xtra"/>
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[[Category: Anthrax lethal factor endopeptidase]]
[[Category: Anthrax lethal factor endopeptidase]]
[[Category: Bacillus anthracis]]
[[Category: Bacillus anthracis]]

Revision as of 11:29, 20 October 2014

Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center

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