4xm6: Difference between revisions

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==Anthrax toxin lethal factor with ligand-induced binding pocket==
==Anthrax toxin lethal factor with ligand-induced binding pocket==
<StructureSection load='4xm6' size='340' side='right' caption='[[4xm6]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='4xm6' size='340' side='right'caption='[[4xm6]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xm6]] 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XM6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XM6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4xm6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XM6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=41R:N~2~-[(4-FLUORO-3-METHYLPHENYL)SULFONYL]-N-HYDROXY-N~2~-(2-METHYLPROPYL)-D-VALINAMIDE'>41R</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.352&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pkq|4pkq]], [[4pkr|4pkr]], [[4pks|4pks]], [[4pkt|4pkt]], [[4pku|4pku]], [[4pkv|4pkv]], [[4pkw|4pkw]], [[4wf6|4wf6]], [[1yqy|1yqy]], [[4xm7|4xm7]], [[4xm8|4xm8]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=41R:N~2~-[(4-FLUORO-3-METHYLPHENYL)SULFONYL]-N-HYDROXY-N~2~-(2-METHYLPROPYL)-D-VALINAMIDE'>41R</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lef, pXO1-107, BXA0172, GBAA_pXO1_0172 ([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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xm6 OCA], [https://pdbe.org/4xm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xm6 RCSB], [https://www.ebi.ac.uk/pdbsum/4xm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xm6 ProSAT]</span></td></tr>
<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>
<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=4xm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xm6 OCA], [http://pdbe.org/4xm6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xm6 RCSB], [http://www.ebi.ac.uk/pdbsum/4xm6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xm6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4xm6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4xm6" style="background-color:#fffaf0;"></div>
==See Also==
*[[Anthrax lethal factor 3D structures|Anthrax lethal factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hydrolase]]
[[Category: Bacillus anthracis]]
[[Category: Finzel, B C]]
[[Category: Large Structures]]
[[Category: Maize, K M]]
[[Category: De la Mora-Rey T]]
[[Category: Mora-Rey, T De la]]
[[Category: Finzel BC]]
[[Category: Anthrax toxin]]
[[Category: Maize KM]]
[[Category: Lethal factor]]
[[Category: Ligand-induced conformational change]]
[[Category: Metalloprotease]]
[[Category: Metalloproteinase]]
[[Category: Structural dynamic]]
[[Category: Toxin]]

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