1a2p: Difference between revisions
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<StructureSection load='1a2p' size='340' side='right'caption='[[1a2p]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1a2p' size='340' side='right'caption='[[1a2p]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a2p]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1a2p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2p OCA], [https://pdbe.org/1a2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2p RCSB], [https://www.ebi.ac.uk/pdbsum/1a2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM]] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Barnase 3D structures|Barnase 3D structures]] | *[[Barnase 3D structures|Barnase 3D structures]] | ||
*[[Ribonuclease|Ribonuclease | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:41, 26 May 2021
BARNASE WILDTYPE STRUCTURE AT 1.5 ANGSTROMS RESOLUTIONBARNASE WILDTYPE STRUCTURE AT 1.5 ANGSTROMS RESOLUTION
Structural highlights
Function[RNBR_BACAM] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of Bacillus amyloliquefaciens ribonuclease (barnase), an extracellular 110-residue enzyme initially solved at 2.0 A resolution, has been refined at 1.5 A using synchrotron radiation and an imaging-plate scanner. Refinement with anisotropic atomic displacement parameters resulted in increased accuracy of the structure. The final model has a crystallographic R factor of 11.5% and an Rfree of 17.4%. The three independent molecules in the asymmetric unit, referred to as A, B and C, allowed detailed analysis of this final model and meaningful comparison with structures of barnase complexed either with nucleotide inhibitors or with its natural intracellular inhibitor, barstar. The analysis of the overall solvent structure revealed a similar number of water molecules associated with each barnase molecule; among these were 16 equivalent buried solvent molecules, the locations of which are discussed in detail and classified on the basis of their structural role. The importance of the water molecules' contribution to the barnase-barstar interaction is also highlighted. The high accuracy of the present analysis revealed the presence of a Zn2+ ion mediating the contacts between pairs of symmetry-related A, B or C molecules; such an ion had previously only been identified for pairs of C molecules. Refinement and structural analysis of barnase at 1.5 A resolution.,Martin C, Richard V, Salem M, Hartley R, Mauguen Y Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):386-98. PMID:10089345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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