1bam: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[1bam]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BAM FirstGlance]. <br>
-</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=1bam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bam OCA], [https://pdbe.org/1bam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bam RCSB], [https://www.ebi.ac.uk/pdbsum/1bam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bam ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</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=1bam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bam OCA], [https://pdbe.org/1bam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bam RCSB], [https://www.ebi.ac.uk/pdbsum/1bam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bam ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/T2BA_BACAM T2BA_BACAM] Recognizes the double-stranded sequence GGATCC and cleaves after G-1.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-BACKGROUND: Type II restriction endonucleases recognize DNA sequences that vary between four to eight base pairs, and require only Mg2+ as a cofactor to catalyze the hydrolysis of DNA. Their protein sequences display a surprising lack of similarity, and no recurring structural motif analogous to the helix-turn-helix or the zinc finger of transcription factors, has yet been discovered. RESULTS: We have determined the crystal structure of restriction endonuclease BamHI at 1.95 A resolution. The structure was solved by combining phase information derived from multi-wavelength X-ray data by algebraic and maximum likelihood methods. The BamHI subunit consists of a central beta-sheet with alpha-helices on both sides. The dimer configuration reveals a large cleft which could accommodate B-form DNA. Mutants of the enzyme that are deficient in cleavage are located at or near the putative DNA-binding cleft. BamHI and endonuclease EcoRI share a common core motif (CCM) consisting of five beta-strands and two helices. It remains to be determined if other restriction enzymes also contain the CCM. CONCLUSIONS: The structure of BamHI provides the first clear evidence that there may be substantial structural homology amongst restriction enzymes, even though it is undetectable at the sequence level.
-Structure of restriction endonuclease bamhi phased at 1.95 A resolution by MAD analysis.,Newman M, Strzelecka T, Dorner LF, Schildkraut I, Aggarwal AK Structure. 1994 May 15;2(5):439-52. PMID:8081758<ref>PMID:8081758</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1bam" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[BamHI|BamHI]]
 *[[Endonuclease 3D structures|Endonuclease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>