2pii
From Proteopedia
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| - | [[Image:2pii.jpg|left|200px]] | + | [[Image:2pii.jpg|left|200px]] |
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| - | '''PII, GLNB PRODUCT''' | + | {{Structure |
| + | |PDB= 2pii |SIZE=350|CAPTION= <scene name='initialview01'>2pii</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= GLNB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''PII, GLNB PRODUCT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PII is a [ | + | 2PII 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=2PII OCA]. |
==Reference== | ==Reference== | ||
| - | X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A., Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:[http:// | + | X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A., Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299730 15299730] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:13:22 2008'' |
Revision as of 16:13, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Gene: | GLNB (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PII, GLNB PRODUCT
Overview
The structure of the bacterial signal transduction protein P(II) has been refined to an R factor of 13.2% using 3sigma data between 10 and 1.9 A. The crystals exhibited twinning by merohedry and X-ray intensities were corrected using the method of Fisher & Sweet [Fisher & Sweet (1980). Acta Cryst. A36, 755-760] prior to refinement. Our earlier 2.7 A structure [Cheah, Carr, Suffolk, Vasudevan, Dixon & Ollis (1994). Structure, 2, 981-990] served as a starting model. P(II) is a trimeric molecule, each subunit has a mass of 12.4 kDa and contains 112 amino-acid residues. The refined model includes all 1065 protein atoms per subunit plus 312 water molecules. The high-resolution refinement confirms the correctness of our 2.7 A model, although it leads to a redefinition of the extent of various secondary-structural elements. The monomeric structure of P(II) exhibits an interlocking double betaalphabeta fold. This is a stable fold found in a number of proteins with diverse functions. The association of the protein into a trimer leads to a new structure which we describe in detail. The effects of crystal packing forces are discussed and potential interaction sites with other proteins and effector molecules are identified.
About this Structure
2PII is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
X-ray structure of the signal transduction protein from Escherichia coli at 1.9 A., Carr PD, Cheah E, Suffolk PM, Vasudevan SG, Dixon NE, Ollis DL, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):93-104. PMID:15299730
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