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| | <StructureSection load='6riy' size='340' side='right'caption='[[6riy]], [[Resolution|resolution]] 1.63Å' scene=''> | | <StructureSection load='6riy' size='340' side='right'caption='[[6riy]], [[Resolution|resolution]] 1.63Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6riy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ccug_50989 Ccug 50989]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RIY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6riy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_intracellulare_subsp._chimaera Mycobacterium intracellulare subsp. chimaera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RIY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.63Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BWK49_00400, MYCOZU1_00080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=222805 CCUG 50989])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=6riy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6riy OCA], [https://pdbe.org/6riy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6riy RCSB], [https://www.ebi.ac.uk/pdbsum/6riy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6riy ProSAT]</span></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=6riy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6riy OCA], [http://pdbe.org/6riy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6riy RCSB], [http://www.ebi.ac.uk/pdbsum/6riy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6riy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/A0A220Y4A5_9MYCO A0A220Y4A5_9MYCO]] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.[ARBA:ARBA00002835][RuleBase:RU362085] | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ccug 50989]] | |
| - | [[Category: DNA helicase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beyer, H M]] | + | [[Category: Mycobacterium intracellulare subsp. chimaera]] |
| - | [[Category: Iwai, H]] | + | [[Category: Beyer HM]] |
| - | [[Category: Lountos, G T]] | + | [[Category: Iwai H]] |
| - | [[Category: Mikula, M K]] | + | [[Category: Lountos GT]] |
| - | [[Category: Wlodawer, A]] | + | [[Category: Mikula MK]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Wlodawer A]] |
| - | [[Category: Intein]]
| + | |
| - | [[Category: Protein-splicing]]
| + | |
| - | [[Category: Splicing]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Protein splicing catalyzed by inteins utilizes many different combinations of amino-acid types at active sites. Inteins have been classified into three classes based on their characteristic sequences. We investigated the structural basis of the protein splicing mechanism of class 3 inteins by determining crystal structures of variants of a class 3 intein from Mycobacterium chimaera and molecular dynamics simulations, which suggested that the class 3 intein utilizes a different splicing mechanism from that of class 1 and 2 inteins. The class 3 intein uses a bond cleavage strategy reminiscent of proteases but share the same Hedgehog/INTein (HINT) fold of other intein classes. Engineering of class 3 inteins from a class 1 intein indicated that a class 3 intein would unlikely evolve directly from a class 1 or 2 intein. The HINT fold appears as structural and functional solution for trans-peptidyl and trans-esterification reactions commonly exploited by diverse mechanisms using different combinations of amino-acid types for the active-site residues.
The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms.,Beyer HM, Virtanen SI, Aranko AS, Mikula KM, Lountos GT, Wlodawer A, Ollila OHS, Iwai H Int J Mol Sci. 2020 Nov 7;21(21). pii: ijms21218367. doi: 10.3390/ijms21218367. PMID:33171880[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Beyer HM, Virtanen SI, Aranko AS, Mikula KM, Lountos GT, Wlodawer A, Ollila OHS, Iwai H. The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms. Int J Mol Sci. 2020 Nov 7;21(21). pii: ijms21218367. doi: 10.3390/ijms21218367. PMID:33171880 doi:http://dx.doi.org/10.3390/ijms21218367
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