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| {{STRUCTURE_2pii| PDB=2pii | SCENE= }} | | {{STRUCTURE_2pii| PDB=2pii | SCENE= }} |
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| '''PII, GLNB PRODUCT'''
| | ===PII, GLNB PRODUCT=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15299730}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15299730 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15299730}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Suffolk, P M.]] | | [[Category: Suffolk, P M.]] |
| [[Category: Signal transduction protein]] | | [[Category: Signal transduction protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:10:45 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:48:43 2008'' |
