1fdm
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdm OCA], [http://www.ebi.ac.uk/pdbsum/1fdm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdm RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FDM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1FDM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_fd Enterobacteria phage fd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDM OCA]. |
==Reference== | ==Reference== | ||
fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix., Almeida FC, Opella SJ, J Mol Biol. 1997 Jul 18;270(3):481-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9237913 9237913] | fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix., Almeida FC, Opella SJ, J Mol Biol. 1997 Jul 18;270(3):481-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9237913 9237913] | ||
| - | [[Category: | + | [[Category: Enterobacteria phage fd]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Almeida, F C.L.]] | [[Category: Almeida, F C.L.]] | ||
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[[Category: micelle]] | [[Category: micelle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:20:53 2008'' |
Revision as of 17:20, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FD MAJOR COAT PROTEIN IN SDS MICELLES, NMR, 20 STRUCTURES
Overview
By performing multidimensional solution NMR experiments on micelle samples it was possible to determine the structure of the membrane-bound form of fd coat protein based on short-range distance and dihedral angle constraints using distance geometry and simulated annealing calculations. Its dynamics were described by 15N relaxation measurements (T1, T2, heteronuclear nuclear Overhauser enhancement (NOE)) fitted with the Lipari-Szabo model-free formalism adapted for the transmembrane and in-plane helices of a membrane protein. The overall correlation time of the protein in micelles was found to be approximately 9 ns, and the local motion of each backbone N-H vector was described by an order parameter and an effective correlation time. The 50 residue protein has an amphipathic alpha-helix (residues 7 to 16) and a hydrophobic alpha-helix (residues 27 to 44), which were found to be approximately perpendicular on the basis of NOEs in the residues that connect the two helices. The residues connecting the helices are of particular interest in membrane proteins, and in this case the loop consists of two turns. The relaxation data show the presence of an extra motion in the amphipathic alpha-helix on the nanosecond timescale and additional flexibility of several residues in the loop connecting the two helices.
About this Structure
1FDM is a Single protein structure of sequence from Enterobacteria phage fd. Full crystallographic information is available from OCA.
Reference
fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix., Almeida FC, Opella SJ, J Mol Biol. 1997 Jul 18;270(3):481-95. PMID:9237913
Page seeded by OCA on Sun Mar 30 20:20:53 2008
