2l0r

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==Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center==
==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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<StructureSection load='2l0r' size='340' side='right'caption='[[2l0r]]' scene=''>
== Structural highlights ==
== 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_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. 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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<table><tr><td colspan='2'>[[2l0r]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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 cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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/Hydrolase Hydrolase], 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'>[https://proteopedia.org/fgij/fg.htm?mol=2l0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0r OCA], [https://pdbe.org/2l0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l0r RCSB], [https://www.ebi.ac.uk/pdbsum/2l0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0r ProSAT]</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://pdbe.org/2l0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l0r RCSB], [http://www.ebi.ac.uk/pdbsum/2l0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l0r ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LEF_BACAN LEF_BACAN]] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.<ref>PMID:9563949</ref> <ref>PMID:9703991</ref> <ref>PMID:10475971</ref> <ref>PMID:11104681</ref> <ref>PMID:10338520</ref>
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[https://www.uniprot.org/uniprot/LEF_BACAN LEF_BACAN] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.<ref>PMID:9563949</ref> <ref>PMID:9703991</ref> <ref>PMID:10475971</ref> <ref>PMID:11104681</ref> <ref>PMID:10338520</ref>
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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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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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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 2l0r" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Anthrax Lethal Factor|Anthrax Lethal Factor]]
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*[[Anthrax lethal factor 3D structures|Anthrax lethal factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hydrolase]]
 
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[[Category: Bentrop, D A]]
 
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[[Category: Chasapis, C T]]
 
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[[Category: Dalkas, G A]]
 
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[[Category: Gkazonis, P V]]
 
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[[Category: Spyroulias, G A]]
 
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[[Category: Anthrax lethal factor]]
 
[[Category: Bacillus anthracis]]
[[Category: Bacillus anthracis]]
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[[Category: Catalytic domain]]
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[[Category: Large Structures]]
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[[Category: Protein]]
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[[Category: Bentrop DA]]
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[[Category: Toxin]]
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[[Category: Chasapis CT]]
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[[Category: Zn metalloprotease]]
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[[Category: Dalkas GA]]
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[[Category: Gkazonis PV]]
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[[Category: Spyroulias GA]]

Current revision

Conformational Dynamics of the Anthrax Lethal Factor Catalytic Center

PDB ID 2l0r

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