4m6f
From Proteopedia
(Difference between revisions)
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| - | + | ==Dimer of the G-Segment Invertase bound to a DNA substrate== | |
| - | + | <StructureSection load='4m6f' size='340' side='right' caption='[[4m6f]], [[Resolution|resolution]] 4.99Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4m6f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M6F FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uj3|3uj3]], [[1gdt|1gdt]], [[3pkz|3pkz]]</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=4m6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m6f RCSB], [http://www.ebi.ac.uk/pdbsum/4m6f PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/DNIV_BPMU DNIV_BPMU]] This protein catalyzes the inversion of a 3000-bp segment of phage DNA. The inversion results in a modification of the 3'-end of the tail fiber gene and alters the host specificity. | [[http://www.uniprot.org/uniprot/DNIV_BPMU DNIV_BPMU]] This protein catalyzes the inversion of a 3000-bp segment of phage DNA. The inversion results in a modification of the 3'-end of the tail fiber gene and alters the host specificity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Crystals of the G-segment invertase in complex with a 37-base-pair asymmetric DNA duplex substrate had an unusually high solvent content of 88% and diffracted to a maximal resolution of about 5.0 A. These crystals exhibited a high degree of non-isomorphism and anisotropy, which presented a serious challenge for structure determination by isomorphous replacement. Here, a procedure of cross-crystal averaging is described that uses large non-isomorphous crystallographic data with a priori information of an approximate molecular boundary as determined from a minimal amount of experimental phase information. Using this procedure, high-quality experimental phases were obtained that have enabled it to be shown that the conformation of the bound substrate DNA duplex significantly differs from those of substrates bound in other serine recombinase-DNA complexes. | ||
| - | + | Exploiting large non-isomorphous differences for phase determination of a G-segment invertase-DNA complex.,Ritacco CJ, Steitz TA, Wang J Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):685-93. doi:, 10.1107/S1399004713032392. Epub 2014 Feb 15. PMID:24598738<ref>PMID:24598738</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Ritacco, C J | + | <references/> |
| - | [[Category: Steitz, T A | + | __TOC__ |
| - | [[Category: Wang, J | + | </StructureSection> |
| + | [[Category: Bpmu]] | ||
| + | [[Category: Ritacco, C J]] | ||
| + | [[Category: Steitz, T A]] | ||
| + | [[Category: Wang, J]] | ||
[[Category: Catalytic domain]] | [[Category: Catalytic domain]] | ||
[[Category: Dna binding domain]] | [[Category: Dna binding domain]] | ||
Revision as of 17:02, 24 December 2014
Dimer of the G-Segment Invertase bound to a DNA substrate
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