3sj1: Difference between revisions

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<StructureSection load='3sj1' size='340' side='right'caption='[[3sj1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3sj1' size='340' side='right'caption='[[3sj1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sj1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51573 Atcc 51573]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SJ1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sj1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51573 Atcc 51573]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SJ1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DXC:(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC+ACID'>DXC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DXC:(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC+ACID'>DXC</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sel|3sel]], [[3sj0|3sj0]], [[3sj4|3sj4]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sel|3sel]], [[3sj0|3sj0]], [[3sj4|3sj4]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ppcA, GSU0612 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35554 ATCC 51573])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ppcA, GSU0612 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35554 ATCC 51573])</td></tr>
<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=3sj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sj1 OCA], [http://pdbe.org/3sj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sj1 RCSB], [http://www.ebi.ac.uk/pdbsum/3sj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sj1 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=3sj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sj1 OCA], [https://pdbe.org/3sj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sj1 RCSB], [https://www.ebi.ac.uk/pdbsum/3sj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sj1 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">

Revision as of 17:51, 3 March 2021

PpcA M58D mutantPpcA M58D mutant

Structural highlights

3sj1 is a 1 chain structure with sequence from Atcc 51573. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:ppcA, GSU0612 (ATCC 51573)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

PpcA is a small protein with 71 residues that contains three covalently bound hemes. The structures of single mutants at residue 58 have shown larger deviations in another part of the protein molecule than at the site of the mutation. Closer examination of the crystal packing has revealed the origin of this unexpected structural change. The site of mutation is within Van der Waals distance from another protein molecule related by a crystallographic twofold axis within the crystal. The structural changes occurred at or near the mutation site have led to a slight adjustment of the surface residues in contact. The observed deviations between the native and the mutant molecular structures are derived from the new crystal packing even though the two crystals are essentially isomorphous. Without careful consideration of the crystal lattice a non-expert looking at only the coordinates deposited in the Protein Data Bank could draw erroneous conclusion that mutation in one part of the molecule affected the structure of the protein in a distant part of the molecule.

Pitfalls in the interpretation of structural changes in mutant proteins from crystal structures.,Pokkuluri PR, Yang X, Londer YY, Schiffer M J Struct Funct Genomics. 2012 Dec;13(4):227-32. doi: 10.1007/s10969-012-9147-1., Epub 2012 Oct 26. PMID:23099666[1]

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

See Also

References

  1. Pokkuluri PR, Yang X, Londer YY, Schiffer M. Pitfalls in the interpretation of structural changes in mutant proteins from crystal structures. J Struct Funct Genomics. 2012 Dec;13(4):227-32. doi: 10.1007/s10969-012-9147-1., Epub 2012 Oct 26. PMID:23099666 doi:http://dx.doi.org/10.1007/s10969-012-9147-1

3sj1, resolution 1.90Å

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OCA