5nxh: Difference between revisions
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<StructureSection load='5nxh' size='340' side='right'caption='[[5nxh]], [[Resolution|resolution]] 2.89Å' scene=''> | <StructureSection load='5nxh' size='340' side='right'caption='[[5nxh]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nxh]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NXH OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5nxh]] is a 3 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=5NXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NXH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5nxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxh OCA], [https://pdbe.org/5nxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nxh RCSB], [https://www.ebi.ac.uk/pdbsum/5nxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxh ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FIBP_BPT4 FIBP_BPT4] Structural component of the proximal-half of the long-tail fiber. The long-tail fibers of T4 are about 1600 Angstroms long with a kink in the middle that divides the fiber into proximal and distal halves.<ref>PMID:8709154</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kanamaru | [[Category: Kanamaru S]] | ||
[[Category: Namura | [[Category: Namura M]] | ||
[[Category: Raaij | [[Category: Van Raaij MJ]] | ||
Latest revision as of 15:14, 22 November 2023
Crystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34, residues 744-1289 at 2.9 Angstrom resolutionCrystal structure of the carboxy-terminal region of the bacteriophage T4 proximal long tail fibre protein gp34, residues 744-1289 at 2.9 Angstrom resolution
Structural highlights
FunctionFIBP_BPT4 Structural component of the proximal-half of the long-tail fiber. The long-tail fibers of T4 are about 1600 Angstroms long with a kink in the middle that divides the fiber into proximal and distal halves.[1] Publication Abstract from PubMedLong tail fibers of bacteriophage T4 are formed by proteins gp34, gp35, gp36, and gp37, with gp34 located at the phage-proximal end and gp37 at the phage-distal, receptor-binding end. We have solved the structure of the carboxy-terminal region of gp34, consisting of amino acids 894-1289, by single-wavelength anomalous diffraction and extended the structure to amino acids 744-1289 using data collected from crystals containing longer gp34-fragments. The structure reveals three repeats of a mixed alpha-beta fibrous domain in residues 744 to 877. A triple-helical neck connects to an extended triple beta-helix domain (amino acids 900-1127) punctuated by two beta-prism domains. Next, a beta-prism domain decorated with short helices and extended beta-helices is present (residues 1146-1238), while the C-terminal end is capped with another short beta-helical region and three beta-hairpins. The structure provides insight into the stability of the fibrous gp34 protein. Crystal Structure of the Carboxy-Terminal Region of the Bacteriophage T4 Proximal Long Tail Fiber Protein Gp34.,Granell M, Namura M, Alvira S, Kanamaru S, van Raaij MJ Viruses. 2017 Jun 30;9(7). pii: E168. doi: 10.3390/v9070168. PMID:28665339[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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