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| | <StructureSection load='6m65' size='340' side='right'caption='[[6m65]], [[Resolution|resolution]] 1.44Å' scene=''> | | <StructureSection load='6m65' size='340' side='right'caption='[[6m65]], [[Resolution|resolution]] 1.44Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6m65]] is a 1 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=6M65 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6M65 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6m65]] is a 1 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=6M65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M65 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 1.44Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_2390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></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=6m65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m65 OCA], [http://pdbe.org/6m65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6m65 RCSB], [http://www.ebi.ac.uk/pdbsum/6m65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6m65 ProSAT]</span></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=6m65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m65 OCA], [https://pdbe.org/6m65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m65 RCSB], [https://www.ebi.ac.uk/pdbsum/6m65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m65 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MUTT1_MYCS2 MUTT1_MYCS2] Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP (PubMed:16585780, PubMed:28375146). At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146). In addition, catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A) (PubMed:28705712).<ref>PMID:16585780</ref> <ref>PMID:28375146</ref> <ref>PMID:28705712</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycs2]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Arif, S M]] | + | [[Category: Arif SM]] |
| - | [[Category: Karthik, S]] | + | [[Category: Karthik S]] |
| - | [[Category: Raj, P]] | + | [[Category: Raj P]] |
| - | [[Category: Varshney, U]] | + | [[Category: Varshney U]] |
| - | [[Category: Vijayan, M]] | + | [[Category: Vijayan M]] |
| - | [[Category: Enzyme action]]
| + | |
| - | [[Category: Gmppnp]]
| + | |
| - | [[Category: Histidine phosphatase domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Molecular aggregation]]
| + | |
| - | [[Category: Msmutt1]]
| + | |
| - | [[Category: Nucleotide pool sanitation enzyme]]
| + | |
| - | [[Category: Nudix hydrolase]]
| + | |
| - | [[Category: Plasticity]]
| + | |
| Structural highlights
6m65 is a 1 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.44Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MUTT1_MYCS2 Catalyzes the conversion of 8-oxo-dGTP to 8-oxo-dGDP, and 8-oxo-GTP to 8-oxo-GDP (PubMed:16585780, PubMed:28375146). At high enzyme concentrations, can also catalyze the conversion of 8-oxo-dGDP to 8-oxo-dGMP, and 8-oxo-GDP to 8-oxo-GMP (PubMed:28375146). In addition, catalyzes the hydrolysis of the diadenosine polyphosphates diadenosine hexaphosphate (Ap6A), diadenosine pentaphosphate (Ap5A) and diadenosine tetraphosphate (Ap4A) (PubMed:28705712).[1] [2] [3]
Publication Abstract from PubMed
Mycobacterium smegmatis MutT1 (MsMutT1) is a sanitation enzyme made up of an N-terminal Nudix hydrolase domain and a C-terminal domain resembling a histidine phosphatase. It has been established that the action of MutT1 on 8-oxo-dGTP, 8-oxo-GTP and diadenosine polyphosphates is modulated by intermolecular interactions. In order to further explore this and to elucidate the structural basis of its differential action on 8-oxo-NTPs and unsubstituted NTPs, the crystal structures of complexes of MsMutT1 with 8-oxo-dGTP, GMPPNP and GMPPCP have been determined. Replacement soaking was used in order to ensure that the complexes were isomorphous to one another. Analysis of the structural data led to the elucidation of a relationship between the arrangements of molecules observed in the crystals, molecular plasticity and the action of the enzyme on nucleotides. The dominant mode of arrangement involving a head-to-tail sequence predominantly leads to the generation of NDPs. The other mode of packing arrangement appears to preferentially generate NMPs. This work also provides interesting insights into the dependence of enzyme action on the conformation of the ligand. The possibility of modulating the enzyme action through differences in intermolecular interactions and ligand conformations makes MsMutT1 a versatile enzyme.
Plasticity, ligand conformation and enzyme action of Mycobacterium smegmatis MutT1.,Raj P, Karthik S, Arif SM, Varshney U, Vijayan M Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):982-992. doi:, 10.1107/S2059798320010992. Epub 2020 Sep 16. PMID:33021500[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dos Vultos T, Blázquez J, Rauzier J, Matic I, Gicquel B. Identification of Nudix hydrolase family members with an antimutator role in Mycobacterium tuberculosis and Mycobacterium smegmatis. J Bacteriol. 2006 Apr;188(8):3159-61. PMID:16585780 doi:10.1128/JB.188.8.3159-3161.2006
- ↑ Arif SM, Patil AG, Varshney U, Vijayan M. Biochemical and structural studies of Mycobacterium smegmatis MutT1, a sanitization enzyme with unusual modes of association. Acta Crystallogr D Struct Biol. 2017 Apr 1;73(Pt 4):349-364. doi:, 10.1107/S2059798317002534. Epub 2017 Mar 31. PMID:28375146 doi:http://dx.doi.org/10.1107/S2059798317002534
- ↑ Arif SM, Varshney U, Vijayan M. Hydrolysis of diadenosine polyphosphates. Exploration of an additional role of Mycobacterium smegmatis MutT1. J Struct Biol. 2017 Jul 10. pii: S1047-8477(17)30122-3. doi:, 10.1016/j.jsb.2017.07.002. PMID:28705712 doi:http://dx.doi.org/10.1016/j.jsb.2017.07.002
- ↑ Raj P, Karthik S, Arif SM, Varshney U, Vijayan M. Plasticity, ligand conformation and enzyme action of Mycobacterium smegmatis MutT1. Acta Crystallogr D Struct Biol. 2020 Oct 1;76(Pt 10):982-992. doi:, 10.1107/S2059798320010992. Epub 2020 Sep 16. PMID:33021500 doi:http://dx.doi.org/10.1107/S2059798320010992
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