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- | {{Seed}} | |
- | [[Image:3m9h.jpg|left|200px]] | |
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- | <!-- | + | ==Crystal structure of the amino terminal coiled coil domain of the Mycobacterium tuberculosis proteasomal ATPase Mpa== |
- | The line below this paragraph, containing "STRUCTURE_3m9h", creates the "Structure Box" on the page.
| + | <StructureSection load='3m9h' size='340' side='right'caption='[[3m9h]], [[Resolution|resolution]] 2.00Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3m9h]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9H FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=3m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9h OCA], [https://pdbe.org/3m9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9h RCSB], [https://www.ebi.ac.uk/pdbsum/3m9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9h ProSAT]</span></td></tr> |
- | {{STRUCTURE_3m9h| PDB=3m9h | SCENE= }}
| + | </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> |
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- | ===Crystal structure of the amino terminal coiled coil domain of the Mycobacterium tuberculosis proteasomal ATPase Mpa=== | + | ==See Also== |
- | | + | *[[ATPase 3D structures|ATPase 3D structures]] |
- | | + | == References == |
- | <!--
| + | <references/> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_20953180}}, adds the Publication Abstract to the page
| + | __TOC__ |
- | (as it appears on PubMed at http://www.pubmed.gov), where 20953180 is the PubMed ID number.
| + | </StructureSection> |
- | -->
| + | [[Category: Large Structures]] |
- | {{ABSTRACT_PUBMED_20953180}}
| + | [[Category: Mycobacterium tuberculosis H37Rv]] |
- | | + | [[Category: Li H]] |
- | ==About this Structure==
| + | [[Category: Wang T]] |
- | 3M9H is a 6 chains structure with sequences from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9H OCA].
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- | | + | |
- | ==Reference== | + | |
- | <ref group="xtra">PMID:20953180</ref><references group="xtra"/> | + | |
- | [[Category: Mycobacterium tuberculosis]] | + | |
- | [[Category: Li, H.]] | + | |
- | [[Category: Wang, T.]] | + | |
- | [[Category: Atp-binding]] | + | |
- | [[Category: Chaperone]]
| + | |
- | [[Category: Four helix antiparallel bundle]]
| + | |
- | [[Category: Nucleotide-binding]]
| + | |
- | [[Category: Proteasome]]
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- | [[Category: S-nitrosylation]]
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- | [[Category: Virulence]]
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- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 27 12:11:04 2010''
| + | |
| Structural highlights
Function
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][1] [2] [3] [4] [5]
See Also
References
- ↑ Darwin KH, Ehrt S, Gutierrez-Ramos JC, Weich N, Nathan CF. The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide. Science. 2003 Dec 12;302(5652):1963-6. PMID:14671303 doi:10.1126/science.1091176
- ↑ Darwin KH, Lin G, Chen Z, Li H, Nathan CF. Characterization of a Mycobacterium tuberculosis proteasomal ATPase homologue. Mol Microbiol. 2005 Jan;55(2):561-71. PMID:15659170 doi:10.1111/j.1365-2958.2004.04403.x
- ↑ Pearce MJ, Arora P, Festa RA, Butler-Wu SM, Gokhale RS, Darwin KH. Identification of substrates of the Mycobacterium tuberculosis proteasome. EMBO J. 2006 Nov 15;25(22):5423-32. PMID:17082771 doi:10.1038/sj.emboj.7601405
- ↑ Wang T, Li H, Lin G, Tang C, Li D, Nathan C, Darwin KH, Li H. Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa. Structure. 2009 Oct 14;17(10):1377-85. PMID:19836337 doi:10.1016/j.str.2009.08.010
- ↑ Striebel F, Hunkeler M, Summer H, Weber-Ban E. The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus. EMBO J. 2010 Apr 7;29(7):1262-71. PMID:20203624 doi:10.1038/emboj.2010.23
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