2vlg

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[[Image:2vlg.jpg|left|200px]]
[[Image:2vlg.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2vlg |SIZE=350|CAPTION= <scene name='initialview01'>2vlg</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2vlg", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Residue+C+1117'>AC1</scene>, <scene name='pdbsite=AC2:Act+Binding+Site+For+Residue+C+1118'>AC2</scene>, <scene name='pdbsite=AC3:Cl+Binding+Site+For+Residue+D+1115'>AC3</scene> and <scene name='pdbsite=AC4:Cl+Binding+Site+For+Residue+B+1115'>AC4</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_kinase Histidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.13.3 2.7.13.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2vlg| PDB=2vlg | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vlg OCA], [http://www.ebi.ac.uk/pdbsum/2vlg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vlg RCSB]</span>
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}}
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'''KINA PAS-A DOMAIN, HOMODIMER'''
'''KINA PAS-A DOMAIN, HOMODIMER'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brautigam, C A.]]
[[Category: Brautigam, C A.]]
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[[Category: Gardner, K.]]
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[[Category: Gardner, K H.]]
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[[Category: Hellingwerf, J.]]
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[[Category: Hellingwerf, K J.]]
[[Category: Kort, R.]]
[[Category: Kort, R.]]
[[Category: Lee, J.]]
[[Category: Lee, J.]]
[[Category: Machius, M.]]
[[Category: Machius, M.]]
[[Category: Tomchick, D R.]]
[[Category: Tomchick, D R.]]
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[[Category: gsic]]
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[[Category: Gsic]]
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[[Category: histidine kinase]]
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[[Category: Histidine kinase]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: pas domain]]
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[[Category: Pas domain]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: scob]]
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[[Category: Scob]]
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[[Category: scod]]
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[[Category: Scod]]
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[[Category: spoiif]]
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[[Category: Spoiif]]
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[[Category: spoiij]]
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[[Category: Spoiij]]
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[[Category: sporulation]]
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[[Category: Sporulation]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: two-component regulatory system]]
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[[Category: Two-component regulatory system]]
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[[Category: two-component signal transduction]]
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[[Category: Two-component signal transduction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 9 14:43:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:13:25 2008''
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Revision as of 11:43, 9 April 2008

Image:2vlg.jpg

Template:STRUCTURE 2vlg

KINA PAS-A DOMAIN, HOMODIMER


Overview

The Bacillus subtilis KinA protein is a histidine protein kinase that controls the commitment of this organism to sporulate in response to nutrient deprivation and several other conditions. Prior studies indicated that the N-terminal Per-ARNT-Sim domain (PAS-A) plays a critical role in the catalytic activity of this enzyme, as demonstrated by the significant decrease of the autophosphorylation rate of a KinA protein lacking this domain. On the basis of the environmental sensing role played by PAS domains in a wide range of proteins, including other bacterial sensor kinases, it has been suggested that the PAS-A domain plays an important regulatory role in KinA function. We have investigated this potential by using a combination of biophysical and biochemical methods to examine PAS-A structure and function, both in isolation and within the intact protein. Here, we present the X-ray crystal structure of the KinA PAS-A domain, showing that it crystallizes as a homodimer using beta-sheet/beta-sheet packing interactions as observed for several other PAS domain complexes. Notably, we observed two dimers with tertiary and quaternary structure differences in the crystalline lattice, indicating significant structural flexibility in these domains. To confirm that KinA PAS-A also forms dimers in solution, we used a combination of NMR spectroscopy, gel filtration chromatography, and analytical ultracentrifugation, the results of which are all consistent with the crystallographic results. We experimentally tested the importance of several residues at the dimer interface using site-directed mutagenesis, finding changes in the PAS-A domain that significantly alter KinA enzymatic activity in vitro and in vivo. These results support the importance of PAS domains within KinA and other histidine kinases and suggest possible routes for natural or artificial regulation of kinase activity.

About this Structure

2VLG is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Changes at the KinA PAS-A Dimerization Interface Influence Histidine Kinase Function(,)., Lee J, Tomchick DR, Brautigam CA, Machius M, Kort R, Hellingwerf KJ, Gardner KH, Biochemistry. 2008 Mar 7;. PMID:18324779 Page seeded by OCA on Wed Apr 9 14:43:28 2008

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