3fc3: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Crystal structure of the beta-beta-alpha-Me type II restriction endonuclease Hpy99I== | ==Crystal structure of the beta-beta-alpha-Me type II restriction endonuclease Hpy99I== | ||
<StructureSection load='3fc3' size='340' side='right' caption='[[3fc3]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='3fc3' size='340' side='right' caption='[[3fc3]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
Line 6: | Line 7: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qnf|2qnf]], [[2qnc|2qnc]], [[1a73|1a73]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qnf|2qnf]], [[2qnc|2qnc]], [[1a73|1a73]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">jhp_0755, synthetic gene codon optimized for Escherichia coli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85963 Campylobacter pylori J99])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">jhp_0755, synthetic gene codon optimized for Escherichia coli ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85963 Campylobacter pylori J99])</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=3fc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fc3 OCA], [http://pdbe.org/3fc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fc3 RCSB], [http://www.ebi.ac.uk/pdbsum/3fc3 PDBsum]</span></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=3fc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fc3 OCA], [http://pdbe.org/3fc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fc3 RCSB], [http://www.ebi.ac.uk/pdbsum/3fc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fc3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Line 27: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 3fc3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3fc3" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 09:38, 1 November 2017
Crystal structure of the beta-beta-alpha-Me type II restriction endonuclease Hpy99ICrystal structure of the beta-beta-alpha-Me type II restriction endonuclease Hpy99I
Structural highlights
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 beta beta alpha-Me restriction endonuclease (REase) Hpy99I recognizes the CGWCG target sequence and cleaves it with unusual stagger (five nucleotide 5'-recessed ends). Here we present the crystal structure of the specific complex of the dimeric enzyme with DNA. The Hpy99I protomer consists of an antiparallel beta-barrel and two beta 4 alpha 2 repeats. Each repeat coordinates a structural zinc ion with four cysteine thiolates in two CXXC motifs. The beta beta alpha-Me region of the second beta 4 alpha 2 repeat holds the catalytic metal ion (or its sodium surrogate) via Asp148 and Asn165 and activates a water molecule with the general base His149. In the specific complex, Hpy99I forms a ring-like structure around the DNA that contacts DNA bases on the major and minor groove sides via the first and second beta 4 alpha 2 repeats, respectively. Hpy99I interacts with the central base pair of the recognition sequence only on the minor groove side, where A:T resembles T:A and G:C is similar to C:G. The Hpy99I-DNA co-crystal structure provides the first detailed illustration of the beta beta alpha-Me site in REases and complements structural information on the use of this active site motif in other groups of endonucleases such as homing endonucleases (e.g. I-PpoI) and Holliday junction resolvases (e.g. T4 endonuclease VII). Crystal structure of the beta beta alpha-Me type II restriction endonuclease Hpy99I with target DNA.,Sokolowska M, Czapinska H, Bochtler M Nucleic Acids Res. 2009 Jun;37(11):3799-810. Epub 2009 Apr 20. PMID:19380375[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|