1x02

From Proteopedia

(Difference between revisions)

Revision as of 16:31, 27 October 2021

Solution structure of stereo array isotope labeled (SAIL) calmodulin

Structural highlights

1x02 is a 1 chain structure with sequence from African clawed frog. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CALM_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.

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

Nuclear-magnetic-resonance spectroscopy can determine the three-dimensional structure of proteins in solution. However, its potential has been limited by the difficulty of interpreting NMR spectra in the presence of broadened and overlapping resonance lines and low signal-to-noise ratios. Here we present stereo-array isotope labelling (SAIL), a technique that can overcome many of these problems by applying a complete stereospecific and regiospecific pattern of stable isotopes that is optimal with regard to the quality and information content of the resulting NMR spectra. SAIL uses exclusively chemically and enzymatically synthesized amino acids for cell-free protein expression. We demonstrate for the 17-kDa protein calmodulin and the 41-kDa maltodextrin-binding protein that SAIL offers sharpened lines, spectral simplification without loss of information, and the ability to rapidly collect the structural restraints required to solve a high-quality solution structure for proteins twice as large as commonly solved by NMR. It thus makes a large class of proteins newly accessible to detailed solution structure determination.

Optimal isotope labelling for NMR protein structure determinations.,Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P Nature. 2006 Mar 2;440(7080):52-7. PMID:16511487^[1]

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

References

↑ Kainosho M, Torizawa T, Iwashita Y, Terauchi T, Mei Ono A, Guntert P. Optimal isotope labelling for NMR protein structure determinations. Nature. 2006 Mar 2;440(7080):52-7. PMID:16511487 doi:10.1038/nature04525

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x02"

@@ Line 3: / Line 3: @@
 <StructureSection load='1x02' size='340' side='right'caption='[[1x02]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1x02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X02 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1x02]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X02 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1x02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x02 OCA], [http://pdbe.org/1x02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x02 RCSB], [http://www.ebi.ac.uk/pdbsum/1x02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x02 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=1x02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x02 OCA], [https://pdbe.org/1x02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x02 RCSB], [https://www.ebi.ac.uk/pdbsum/1x02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x02 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
+[[https://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1x02

From Proteopedia

Revision as of 16:31, 27 October 2021

Solution structure of stereo array isotope labeled (SAIL) calmodulin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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