1brg

<StructureSection load='1brg' size='340' side='right' caption='[[1brg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1brg]] is a 3 chain structure with sequence from [http://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=1BRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BRG 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>

<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=1brg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brg OCA], [http://pdbe.org/1brg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1brg RCSB], [http://www.ebi.ac.uk/pdbsum/1brg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1brg ProSAT]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brg_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The crystal structure of a barnase mutant, Phe--&gt;Leu7 has been determined to 2.2 A resolution. No structural rearrangement is observed near the mutated residue. The F7L mutation is highly destabilizing and this is caused by the loss of extensive van der Waals contacts that wild-type Phe7 made with its neighbouring residues, and the exposure of a large hydrophobic pocket on the surface of the protein. The side-chain conformations of the mutated Leu7 residue have torsion angles chi(1) ranging from -138 degrees to -168 degrees and chi(2) ranging from +16 degrees to +70 degrees, for the three molecules in the asymmetric unit. These angles do not agree with the most frequently observed conformations in the protein side-chain rotamer library [Ponder &amp; Richards (1987). J. Mol. Biol. 193, 775-791]. However, when compared to a more recent 'backbone-dependent' rotamer library [Dunbrack &amp; Karplus (1993). J. Mol. Biol. 230, 543-574], the side-chain conformation of Leu7 agrees well with that of the most frequently observed rotamers. The side-chain conformation of Leu7 was found to be dictated by two factors: it has the lowest conformational energy and it buries the most hydrophobic surface area.

Crystallographic analysis of Phe--&gt;Leu substitution in the hydrophobic core of barnase.,Chen YW, Fersht AR, Henrick K Acta Crystallogr D Biol Crystallogr. 1995 Mar 1;51(Pt 2):220-31. PMID:15299323<ref>PMID:15299323</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1brg" style="background-color:#fffaf0;"></div>

*[[Temp|Temp]]

[[Category: Chen, Y W]]

[[Category: Fersht, A R]]

[[Category: Henrick, K]]

[[Category: Endonuclease]]