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[[Image: | ==ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM== | ||
<StructureSection load='1gmg' size='340' side='right' caption='[[1gmg]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gmg]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GMG FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b6q|1b6q]], [[1f4m|1f4m]], [[1f4n|1f4n]], [[1gto|1gto]], [[1nkd|1nkd]], [[1rop|1rop]], [[1rpo|1rpo]], [[1rpr|1rpr]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gmg RCSB], [http://www.ebi.ac.uk/pdbsum/1gmg PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/1gmg_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:12657790</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Rop protein|Rop protein]] | *[[Rop protein|Rop protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Glykos, N M.]] | [[Category: Glykos, N M.]] | ||
[[Category: Kokkinidis, M.]] | [[Category: Kokkinidis, M.]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
Revision as of 11:42, 28 September 2014
ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORMALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM
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 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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