3fp9: Difference between revisions

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 <StructureSection load='3fp9' size='340' side='right'caption='[[3fp9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fp9]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FP9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3FP9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fp9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FP9 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3fp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fp9 OCA], [http://pdbe.org/3fp9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fp9 RCSB], [http://www.ebi.ac.uk/pdbsum/3fp9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fp9 ProSAT]</span></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&#8491;</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=3fp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fp9 OCA], [https://pdbe.org/3fp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fp9 RCSB], [https://www.ebi.ac.uk/pdbsum/3fp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fp9 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ARC_MYCTU ARC_MYCTU] ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Is required but not sufficient to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types.[HAMAP-Rule:MF_02112]<ref>PMID:14671303</ref> <ref>PMID:15659170</ref> <ref>PMID:17082771</ref> <ref>PMID:19836337</ref> <ref>PMID:20203624</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 19: @@
 </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=3fp9 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Proteasome-mediated protein turnover in all domains of life is an energy-dependent process that requires ATPase activity. Mycobacterium tuberculosis (Mtb) was recently shown to possess a ubiquitin-like proteasome pathway that plays an essential role in Mtb resistance to killing by products of host macrophages. Here we report our structural and biochemical investigation of Mpa, the presumptive Mtb proteasomal ATPase. We demonstrate that Mpa binds to the Mtb proteasome in the presence of ATPgammaS, providing the physical evidence that Mpa is the proteasomal ATPase. X-ray crystallographic determination of the conserved interdomain showed a five stranded double beta barrel structure containing a Greek key motif. Structure and mutational analysis indicate a major role of the interdomain for Mpa hexamerization. Our mutational and functional studies further suggest that the central channel in the Mpa hexamer is involved in protein substrate translocation and degradation. These studies provide insights into how a bacterial proteasomal ATPase interacts with and facilitates protein degradation by the proteasome.
-Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa.,Wang T, Li H, Lin G, Tang C, Li D, Nathan C, Darwin KH, Li H Structure. 2009 Oct 14;17(10):1377-85. PMID:19836337<ref>PMID:19836337</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3fp9" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 34: / Line 28: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Li, H]]
+[[Category: Mycobacterium tuberculosis]]
-[[Category: Wang, T]]
+[[Category: Li H]]
-[[Category: Aaa atpase]]
+[[Category: Wang T]]
-[[Category: Atp-binding]]
-[[Category: Five strand beta barrel]]
-[[Category: Hexamer]]
-[[Category: Hydrolase]]
-[[Category: Nucleotide-binding]]
-[[Category: Proteasomal atpase]]