1gmg: Difference between revisions
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<StructureSection load='1gmg' size='340' side='right'caption='[[1gmg]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1gmg' size='340' side='right'caption='[[1gmg]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gmg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GMG FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gmg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GMG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=1gmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmg OCA], [https://pdbe.org/1gmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gmg RCSB], [https://www.ebi.ac.uk/pdbsum/1gmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gmg ProSAT]</span></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=1gmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmg OCA], [https://pdbe.org/1gmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gmg RCSB], [https://www.ebi.ac.uk/pdbsum/1gmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gmg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Glykos | [[Category: Glykos NM]] | ||
[[Category: Kokkinidis | [[Category: Kokkinidis M]] | ||
Revision as of 15:00, 13 December 2023
ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORMALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM
Structural highlights
FunctionROP_ECOLX Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events. 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 crystal structure of a 4-alpha-helical bundle protein has been determined by the application of a 23-dimensional molecular-replacement search performed using a stochastic method. The search model for the calculation was a 26-residue-long polyalanine helix amounting to less than 13% of the total number of atoms in the asymmetric unit of the target crystal structure. The crystal structure determination procedure is presented in detail, with emphasis on the molecular-replacement calculations. Structure determination of a small protein through a 23-dimensional molecular-replacement search.,Glykos NM, Kokkinidis M Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):709-18. Epub 2003, Mar 25. PMID:12657790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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