1aa0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1aa0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aa0, resolution 2.2&Aring;" /> '''FIBRITIN DELETION MUT...)
Current revision (06:28, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1aa0.gif|left|200px]]<br /><applet load="1aa0" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1aa0, resolution 2.2&Aring;" />
 
-
'''FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)'''<br />
 
-
==Overview==
+
==FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)==
-
BACKGROUND: Oligomeric coiled-coil motifs are found in numerous protein, structures; among them is fibritin, a structural protein of bacteriophage, T4, which belongs to a class of chaperones that catalyze a specific, phage-assembly process. Fibritin promotes the assembly of the long tail, fibers and their subsequent attachment to the tail baseplate; it is also a, sensing device that controls the retraction of the long tail fibers in, adverse environments and, thus, prevents infection. The structure of, fibritin had been predicted from sequence and biochemical analyses to be, mainly a triple-helical coiled coil. The determination of its structure at, atomic resolution was expected to give insights into the assembly process, and biological function of fibritin, and the properties of modified, coiled-coil structures in general. RESULTS: The three-dimensional, structure of fibritin E, a deletion mutant of wild-type fibritin, was, determined to 2.2 A resolution by X-ray crystallography. Three identical, subunits of 119 amino acid residues form a trimeric parallel coiled-coil, domain and a small globular C-terminal domain about a crystallographic, threefold axis. The coiled-coil domain is divided into three segments that, are separated by insertion loops. The C-terminal domain, which consists of, 30 residues from each subunit, contains a beta-propeller-like structure, with a hydrophobic interior. CONCLUSIONS: The residues within the, C-terminal domain make extensive hydrophobic and some polar intersubunit, interactions. This is consistent with the C-terminal domain being, important for the correct assembly of fibritin, as shown earlier by, mutational studies. Tight interactions between the C-terminal residues of, adjacent subunits counteract the latent instability that is suggested by, the structural properties of the coiled-coil segments. Trimerization is, likely to begin with the formation of the C-terminal domain which, subsequently initiates the assembly of the coiled coil. The interplay, between the stabilizing effect of the C-terminal domain and the labile, coiled-coil domain may be essential for the fibritin function and for the, correct functioning of many other alpha-fibrous proteins.
+
<StructureSection load='1aa0' size='340' side='right'caption='[[1aa0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1aa0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AA0 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa0 OCA], [https://pdbe.org/1aa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aa0 RCSB], [https://www.ebi.ac.uk/pdbsum/1aa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aa0 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').
-
==About this Structure==
+
==See Also==
-
1AA0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CL and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AA0 OCA].
+
*[[Fibritin|Fibritin]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain., Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG, Structure. 1997 Jun 15;5(6):789-98. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9261070 9261070]
+
[[Category: Escherichia virus T4]]
-
[[Category: Bacteriophage t4]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Mesyanzhinov VV]]
-
[[Category: Mesyanzhinov, V.V.]]
+
[[Category: Rossmann MG]]
-
[[Category: Rossmann, M.G.]]
+
[[Category: Strelkov SV]]
-
[[Category: Strelkov, S.V.]]
+
[[Category: Tao Y]]
-
[[Category: Tao, Y.]]
+
-
[[Category: CL]]
+
-
[[Category: ZN]]
+
-
[[Category: attachment protein]]
+
-
[[Category: bacteriophage assembly]]
+
-
[[Category: bacteriophage t4]]
+
-
[[Category: coiled coil]]
+
-
[[Category: fibritin]]
+
-
[[Category: structural protein]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:42:43 2007''
+

Current revision

FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)

PDB ID 1aa0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aa0"
Personal tools