1wcr: Difference between revisions

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[[Image:1wcr.gif|left|200px]]<br /><applet load="1wcr" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1wcr.gif|left|200px]]
caption="1wcr" />
 
'''TRIMERIC STRUCTURE OF THE ENZYME IIA FROM ESCHERICHIA COLI PHOSPHOTRANSFERASE SYSTEM SPECIFIC FOR N,N'-DIACETYLCHITOBIOSE'''<br />
{{Structure
|PDB= 1wcr |SIZE=350|CAPTION= <scene name='initialview01'>1wcr</scene>
|SITE=  
|LIGAND=  
|ACTIVITY= [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69]
|GENE=
}}
 
'''TRIMERIC STRUCTURE OF THE ENZYME IIA FROM ESCHERICHIA COLI PHOSPHOTRANSFERASE SYSTEM SPECIFIC FOR N,N'-DIACETYLCHITOBIOSE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1WCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCR OCA].  
1WCR is a [[Single protein]] structure of 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=1WCR OCA].  


==Reference==
==Reference==
Solution structure of enzyme IIA(Chitobiose) from the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system., Tang C, Williams DC Jr, Ghirlando R, Clore GM, J Biol Chem. 2005 Mar 25;280(12):11770-80. Epub 2005 Jan 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15654077 15654077]
Solution structure of enzyme IIA(Chitobiose) from the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system., Tang C, Williams DC Jr, Ghirlando R, Clore GM, J Biol Chem. 2005 Mar 25;280(12):11770-80. Epub 2005 Jan 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15654077 15654077]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
[[Category: Protein-N(pi)-phosphohistidine--sugar phosphotransferase]]
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[[Category: mutagenesis]]
[[Category: mutagenesis]]
[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
[[Category: pts]]
[[Category: pt]]
[[Category: sugar transport]]
[[Category: sugar transport]]
[[Category: transferase]]
[[Category: transferase]]


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Revision as of 15:55, 20 March 2008

File:1wcr.gif


PDB ID 1wcr

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Activity: Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69
Coordinates: save as pdb, mmCIF, xml



TRIMERIC STRUCTURE OF THE ENZYME IIA FROM ESCHERICHIA COLI PHOSPHOTRANSFERASE SYSTEM SPECIFIC FOR N,N'-DIACETYLCHITOBIOSE


OverviewOverview

The solution structure of trimeric Escherichia coli enzyme IIA(Chb) (34 kDa), a component of the N,N'-diacetylchitobiose/lactose branch of the phosphotransferase signal transduction system, has been determined by NMR spectroscopy. Backbone residual dipolar couplings were used to provide long range orientational restraints, and long range (|i - j| > or = 5 residues) nuclear Overhauser enhancement restraints were derived exclusively from samples in which at least one subunit was 15N/13C/2H/(Val-Leu-Ile)-methyl-protonated. Each subunit consists of a three-helix bundle. Hydrophobic residues lining helix 3 of each subunit are largely responsible for the formation of a parallel coiled-coil trimer. The active site histidines (His-89 from each subunit) are located in three symmetrically placed deep crevices located at the interface of two adjacent subunits (A and C, C and B, and B and A). Partially shielded from bulk solvent, structural modeling suggests that phosphorylated His-89 is stabilized by electrostatic interactions with the side chains of His-93 from the same subunit and Gln-91 from the adjacent subunit. Comparison with the x-ray structure of Lactobacillus lactis IIA(Lac) reveals some substantial structural differences, particularly in regard to helix 3, which exhibits a 40 degrees kink in IIA(Lac) versus a 7 degrees bend in IIA(Chb). This is associated with the presence of an unusually large (230-angstroms3) buried hydrophobic cavity at the trimer interface in IIA(Lac) that is reduced to only 45 angstroms3) in IIA(Chb).

About this StructureAbout this Structure

1WCR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of enzyme IIA(Chitobiose) from the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system., Tang C, Williams DC Jr, Ghirlando R, Clore GM, J Biol Chem. 2005 Mar 25;280(12):11770-80. Epub 2005 Jan 14. PMID:15654077

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