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==Crystal structure of a retropepsin-like aspartic protease from Rickettsia conorii== | ==Crystal structure of a retropepsin-like aspartic protease from Rickettsia conorii== | ||
<StructureSection load='5c9b' size='340' side='right' caption='[[5c9b]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='5c9b' size='340' side='right' caption='[[5c9b]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c9b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C9B FirstGlance]. <br> | <table><tr><td colspan='2'>[[5c9b]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_vr-613 Atcc vr-613]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C9B FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c9d|5c9d]], [[5c9f|5c9f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c9d|5c9d]], [[5c9f|5c9f]]</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=5c9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c9b OCA], [http://pdbe.org/5c9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c9b RCSB], [http://www.ebi.ac.uk/pdbsum/5c9b PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RC1339 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=781 ATCC VR-613])</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=5c9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c9b OCA], [http://pdbe.org/5c9b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c9b RCSB], [http://www.ebi.ac.uk/pdbsum/5c9b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c9b ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure of the decadeoxyribonucleotide d(GCATGCATGC) is presented at a resolution of 1.8 A. The decamer adopts a novel double-folded structure in which the direction of progression of the backbone changes at the two thymine residues. Intra-strand stacking interactions (including an interaction between the endocylic O atom of a ribose moiety and the adjacent purine base), hydrogen bonds and cobalt-ion interactions stabilize the double-folded structure of the single strand. Two such double-folded strands come together in the crystal to form a dimer. Inter-strand Watson-Crick hydrogen bonds form four base pairs. This portion of the decamer structure is similar to that observed in other previously reported oligonucleotide structures and has been dubbed a `bi-loop'. Both the double-folded single-strand structure, as well as the dimeric bi-loop structure, serve as starting points to construct models for triplet-repeat DNA sequences, which have been implicated in many human diseases. | |||
The novel double-folded structure of d(GCATGCATGC): a possible model for triplet-repeat sequences.,Thirugnanasambandam A, Karthik S, Mandal PK, Gautham N Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):2119-26. doi:, 10.1107/S1399004715013930. Epub 2015 Sep 30. PMID:26457435<ref>PMID:26457435</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5c9b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc vr-613]] | |||
[[Category: Cruz, R]] | [[Category: Cruz, R]] | ||
[[Category: Curto, P]] | [[Category: Curto, P]] | ||
Revision as of 09:17, 18 April 2018
Crystal structure of a retropepsin-like aspartic protease from Rickettsia conoriiCrystal structure of a retropepsin-like aspartic protease from Rickettsia conorii
Structural highlights
Publication Abstract from PubMedThe structure of the decadeoxyribonucleotide d(GCATGCATGC) is presented at a resolution of 1.8 A. The decamer adopts a novel double-folded structure in which the direction of progression of the backbone changes at the two thymine residues. Intra-strand stacking interactions (including an interaction between the endocylic O atom of a ribose moiety and the adjacent purine base), hydrogen bonds and cobalt-ion interactions stabilize the double-folded structure of the single strand. Two such double-folded strands come together in the crystal to form a dimer. Inter-strand Watson-Crick hydrogen bonds form four base pairs. This portion of the decamer structure is similar to that observed in other previously reported oligonucleotide structures and has been dubbed a `bi-loop'. Both the double-folded single-strand structure, as well as the dimeric bi-loop structure, serve as starting points to construct models for triplet-repeat DNA sequences, which have been implicated in many human diseases. The novel double-folded structure of d(GCATGCATGC): a possible model for triplet-repeat sequences.,Thirugnanasambandam A, Karthik S, Mandal PK, Gautham N Acta Crystallogr D Biol Crystallogr. 2015 Oct;71(Pt 10):2119-26. doi:, 10.1107/S1399004715013930. Epub 2015 Sep 30. PMID:26457435[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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