1gmg: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:


==ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM==
==ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM==
<StructureSection load='1gmg' size='340' side='right' caption='[[1gmg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1gmg' size='340' side='right'caption='[[1gmg]], [[Resolution|resolution]] 1.90&Aring;' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GMG FirstGlance]. <br>
<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GMG FirstGlance]. <br>
Line 13: Line 13:
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gm/1gmg_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 35: Line 35:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Glykos, N M]]
[[Category: Glykos, N M]]
[[Category: Kokkinidis, M]]
[[Category: Kokkinidis, M]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]

Revision as of 11:24, 26 June 2019

ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORMALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM

Structural highlights

1gmg is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Glykos NM, Kokkinidis M. Structure determination of a small protein through a 23-dimensional molecular-replacement search. Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):709-18. Epub 2003, Mar 25. PMID:12657790

1gmg, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA