3lt3: Difference between revisions

Latest revision as of 08:43, 6 September 2023

Crystal structure of Rv3671c from M. tuberculosis H37Rv, Ser343Ala mutant, inactive form

Structural highlights

3lt3 is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Y3671_MYCTU Required for M.tuberculosis resistance to oxidative stress in addition to its role in resistance to acid, which is essential for virulence. It protects M.tuberculosis against phagolysosomal concentrations of acid and maintains its intrabacterial pH when phagocytosed by IFN-gamma-activated macrophages.^[1] ^[2]

Publication Abstract from PubMed

Rv3671c, a putative serine protease, is crucial for persistence of Mycobacterium tuberculosis in the hostile environment of the phagosome. We show that Rv3671c is required for M. tuberculosis resistance to oxidative stress in addition to its role in protection from acidification. Structural and biochemical analyses demonstrate that the periplasmic domain of Rv3671c is a functional serine protease of the chymotrypsin family and, remarkably, that its activity increases on oxidation. High-resolution crystal structures of this protease in an active strained state and in an inactive relaxed state reveal that a solvent-exposed disulfide bond controls the protease activity by constraining two distant regions of Rv3671c and stabilizing it in the catalytically active conformation. In vitro biochemical studies confirm that activation of the protease in an oxidative environment is dependent on this reversible disulfide bond. These results suggest that the disulfide bond modulates activity of Rv3671c depending on the oxidative environment in vivo.

Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.,Biswas T, Small J, Vandal O, Odaira T, Deng H, Ehrt S, Tsodikov OV Structure. 2010 Oct 13;18(10):1353-63. PMID:20947023^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Vandal OH, Pierini LM, Schnappinger D, Nathan CF, Ehrt S. A membrane protein preserves intrabacterial pH in intraphagosomal Mycobacterium tuberculosis. Nat Med. 2008 Aug;14(8):849-54. doi: 10.1038/nm.1795. Epub 2008 Jul 20. PMID:18641659 doi:https://dx.doi.org/10.1038/nm.1795
↑ Biswas T, Small J, Vandal O, Odaira T, Deng H, Ehrt S, Tsodikov OV. Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress. Structure. 2010 Oct 13;18(10):1353-63. PMID:20947023 doi:10.1016/j.str.2010.06.017
↑ Biswas T, Small J, Vandal O, Odaira T, Deng H, Ehrt S, Tsodikov OV. Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress. Structure. 2010 Oct 13;18(10):1353-63. PMID:20947023 doi:10.1016/j.str.2010.06.017

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Vandal OH, Pierini LM, Schnappinger D, Nathan CF, Ehrt S. A membrane protein preserves intrabacterial pH in intraphagosomal Mycobacterium tuberculosis. Nat Med. 2008 Aug;14(8):849-54. doi: 10.1038/nm.1795. Epub 2008 Jul 20. PMID:18641659 doi:https://dx.doi.org/10.1038/nm.1795

[2] Biswas T, Small J, Vandal O, Odaira T, Deng H, Ehrt S, Tsodikov OV. Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress. Structure. 2010 Oct 13;18(10):1353-63. PMID:20947023 doi:10.1016/j.str.2010.06.017

[3] Biswas T, Small J, Vandal O, Odaira T, Deng H, Ehrt S, Tsodikov OV. Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress. Structure. 2010 Oct 13;18(10):1353-63. PMID:20947023 doi:10.1016/j.str.2010.06.017

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='3lt3' size='340' side='right'caption='[[3lt3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lt3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LT3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lt3]] is a 2 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=3LT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LT3 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k6y|3k6y]], [[3k6z|3k6z]]</div></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]] 2.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT3772, Rv3671c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=3lt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lt3 OCA], [https://pdbe.org/3lt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lt3 RCSB], [https://www.ebi.ac.uk/pdbsum/3lt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lt3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/Y3671_MYCTU Y3671_MYCTU]] Required for M.tuberculosis resistance to oxidative stress in addition to its role in resistance to acid, which is essential for virulence. It protects M.tuberculosis against phagolysosomal concentrations of acid and maintains its intrabacterial pH when phagocytosed by IFN-gamma-activated macrophages.<ref>PMID:18641659</ref> <ref>PMID:20947023</ref>
+[https://www.uniprot.org/uniprot/Y3671_MYCTU Y3671_MYCTU] Required for M.tuberculosis resistance to oxidative stress in addition to its role in resistance to acid, which is essential for virulence. It protects M.tuberculosis against phagolysosomal concentrations of acid and maintains its intrabacterial pH when phagocytosed by IFN-gamma-activated macrophages.<ref>PMID:18641659</ref> <ref>PMID:20947023</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Myctu]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Biswas, T]]
+[[Category: Biswas T]]
-[[Category: Ehrt, S]]
+[[Category: Ehrt S]]
-[[Category: Small, J]]
+[[Category: Small J]]
-[[Category: Tsodikov, O V]]
+[[Category: Tsodikov OV]]
-[[Category: Vandal, O]]
+[[Category: Vandal O]]
-[[Category: H37rv]]
-[[Category: Htra]]
-[[Category: Hydrolase]]
-[[Category: Protease]]
-[[Category: Serine protease]]

3lt3: Difference between revisions

Latest revision as of 08:43, 6 September 2023

Crystal structure of Rv3671c from M. tuberculosis H37Rv, Ser343Ala mutant, inactive form

Structural highlights

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Publication Abstract from PubMed

References

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