1fdm: Difference between revisions
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<StructureSection load='1fdm' size='340' side='right' caption='[[1fdm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1fdm' size='340' side='right' caption='[[1fdm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fdm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1fdm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpfd Bpfd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FDM FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1fdm RCSB], [http://www.ebi.ac.uk/pdbsum/1fdm PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1fdm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fdm RCSB], [http://www.ebi.ac.uk/pdbsum/1fdm PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://www.uniprot.org/uniprot/CAPSD_BPFD CAPSD_BPFD]] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1fdm" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bpfd]] | ||
[[Category: Almeida, F C.L]] | [[Category: Almeida, F C.L]] | ||
[[Category: Opella, S J]] | [[Category: Opella, S J]] | ||
Revision as of 15:05, 11 September 2015
FD MAJOR COAT PROTEIN IN SDS MICELLES, NMR, 20 STRUCTURESFD MAJOR COAT PROTEIN IN SDS MICELLES, NMR, 20 STRUCTURES
Structural highlights
Function[CAPSD_BPFD] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). Publication Abstract from PubMedBy 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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