6cum

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==Crystal structure of a C-terminal proteolytic fragment of a protein annotated as an LAO/AO transport system ATPase but likely MeaB and MMAA-like GTPase from Mycobacterium smegmatis==
==Crystal structure of a C-terminal proteolytic fragment of a protein annotated as an LAO/AO transport system ATPase but likely MeaB and MMAA-like GTPase from Mycobacterium smegmatis==
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<StructureSection load='6cum' size='340' side='right' caption='[[6cum]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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<StructureSection load='6cum' size='340' side='right'caption='[[6cum]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6cum]] 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=6CUM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CUM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6cum]] 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=6CUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CUM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_4869 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cum OCA], [http://pdbe.org/6cum PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cum RCSB], [http://www.ebi.ac.uk/pdbsum/6cum PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cum ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cum OCA], [https://pdbe.org/6cum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cum RCSB], [https://www.ebi.ac.uk/pdbsum/6cum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cum ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0R1T8_MYCS2 A0R1T8_MYCS2]
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Crystal structure determination requires solving the phase problem. This can be accomplished using ab initio direct methods for small molecules and macromolecules at resolutions higher than 1.2 A, whereas macromolecular structure determination at lower resolution requires either molecular replacement using a homologous structure or experimental phases using a derivative such as covalent labeling (for example selenomethionine or mercury derivatization) or heavy-atom soaking (for example iodide ions). Here, a case is presented in which crystals were obtained from a 30.8 kDa protein sample and yielded a 1.6 A resolution data set with a unit cell that could accommodate approximately 8 kDa of protein. Thus, it was unclear what had been crystallized. Molecular replacement with pieces of homologous proteins and attempts at iodide ion soaking failed to yield a solution. The crystals could not be reproduced. Sequence-independent molecular replacement using the structures available in the Protein Data Bank also failed to yield a solution. Ultimately, ab initio structure solution proved successful using the program ARCIMBOLDO, which identified two alpha-helical elements and yielded interpretable maps. The structure was the C-terminal dimerization domain of the intended target from Mycobacterium smegmatis. This structure is presented as a user-friendly test case in which an unknown protein fragment could be determined using ARCIMBOLDO.
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Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO.,Abendroth J, Sankaran B, Myler PJ, Lorimer DD, Edwards TE Acta Crystallogr F Struct Biol Commun. 2018 Sep 1;74(Pt 9):530-535. doi:, 10.1107/S2053230X18010063. Epub 2018 Aug 29. PMID:30198884<ref>PMID:30198884</ref>
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6cum" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycs2]]
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[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Mycolicibacterium smegmatis MC2 155]]
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[[Category: Proteolytic fragment]]
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[[Category: Ssgcid]]
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[[Category: Transferase]]
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Crystal structure of a C-terminal proteolytic fragment of a protein annotated as an LAO/AO transport system ATPase but likely MeaB and MMAA-like GTPase from Mycobacterium smegmatis

PDB ID 6cum

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