7bx8

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<StructureSection load='7bx8' size='340' side='right'caption='[[7bx8]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='7bx8' size='340' side='right'caption='[[7bx8]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7bx8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BX8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BX8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7bx8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BX8 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[7bwr|7bwr]]</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">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">embB, MSMEI_6221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2]), acpM, MSMEG_4326, MSMEI_4226 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=7bx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bx8 OCA], [https://pdbe.org/7bx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bx8 RCSB], [https://www.ebi.ac.uk/pdbsum/7bx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bx8 ProSAT]</span></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/Indolylacetylinositol_arabinosyltransferase Indolylacetylinositol arabinosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.34 2.4.2.34] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7bx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bx8 OCA], [http://pdbe.org/7bx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bx8 RCSB], [http://www.ebi.ac.uk/pdbsum/7bx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bx8 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ACPM_MYCS2 ACPM_MYCS2]] Acyl carrier protein involved in meromycolate extension.
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[https://www.uniprot.org/uniprot/A0R614_MYCS2 A0R614_MYCS2] Arabinosyl transferase responsible for the polymerization of arabinose into the arabinan of arabinogalactan.[ARBA:ARBA00003001]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Inhibition of Mycobacterium tuberculosis (Mtb) cell wall assembly is an established strategy for anti-TB chemotherapy. Arabinosyltransferase EmbB, which catalyzes the transfer of arabinose from the donor decaprenyl-phosphate-arabinose (DPA) to its arabinosyl acceptor is an essential enzyme for Mtb cell wall synthesis. Analysis of drug resistance mutations suggests that EmbB is the main target of the front-line anti-TB drug, ethambutol. Herein, we report the cryo-EM structures of Mycobacterium smegmatis EmbB in its "resting state" and DPA-bound "active state". EmbB is a fifteen-transmembrane-spanning protein, assembled as a dimer. Each protomer has an associated acyl-carrier-protein (AcpM) on their cytoplasmic surface. Conformational changes upon DPA binding indicate an asymmetric movement within the EmbB dimer during catalysis. Functional studies have identified critical residues in substrate recognition and catalysis, and demonstrated that ethambutol inhibits transferase activity of EmbB by competing with DPA. The structures represent the first step directed towards a rational approach for anti-TB drug discovery.
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Cryo-EM snapshots of mycobacterial arabinosyltransferase complex EmbB2-AcpM2.,Zhang L, Zhao Y, Gao R, Li J, Yang X, Gao Y, Zhao W, Gurcha SS, Veerapen N, Batt SM, Besra KK, Xu W, Bi L, Zhang X, Guddat LW, Yang H, Wang Q, Besra GS, Rao Z Protein Cell. 2020 May 3. pii: 10.1007/s13238-020-00726-6. doi:, 10.1007/s13238-020-00726-6. PMID:32363534<ref>PMID:32363534</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 7bx8" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Indolylacetylinositol arabinosyltransferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mycs2]]
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[[Category: Mycolicibacterium smegmatis MC2 155]]
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[[Category: Gao, R G]]
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[[Category: Gao RG]]
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[[Category: Rao, Z H]]
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[[Category: Rao ZH]]
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[[Category: Wang, Q]]
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[[Category: Wang Q]]
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[[Category: Zhang, L]]
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[[Category: Zhang L]]
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[[Category: Acyl-carrier-protein]]
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[[Category: Arabinoglacatan]]
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[[Category: Arabinosyltransferase]]
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[[Category: Cell wall synthesis]]
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[[Category: Cryo-em]]
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[[Category: Embb]]
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[[Category: Ethambutol]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Transferase]]
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Current revision

Mycobacterium smegmatis arabinosyltransferase complex EmbB2-AcpM2 in symmetric "resting state"

PDB ID 7bx8

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