1v8z: Difference between revisions

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[[Image:1v8z.gif|left|200px]]
[[Image:1v8z.gif|left|200px]]


{{Structure
<!--
|PDB= 1v8z |SIZE=350|CAPTION= <scene name='initialview01'>1v8z</scene>, resolution 2.21&Aring;
The line below this paragraph, containing "STRUCTURE_1v8z", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span>
or leave the SCENE parameter empty for the default display.
|GENE= TrpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])
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|DOMAIN=
{{STRUCTURE_1v8z|  PDB=1v8z |  SCENE= }}  
|RELATEDENTRY=[[1geq|1GEQ]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v8z OCA], [http://www.ebi.ac.uk/pdbsum/1v8z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v8z RCSB]</span>
}}


'''X-ray crystal structure of the Tryptophan Synthase b2 Subunit from Hyperthermophile, Pyrococcus furiosus'''
'''X-ray crystal structure of the Tryptophan Synthase b2 Subunit from Hyperthermophile, Pyrococcus furiosus'''
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[[Category: Yamagata, Y.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
[[Category: beta+alpha]]
[[Category: Beta+alpha]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: Rsgi]]
[[Category: structural genomic]]
[[Category: Structural genomic]]
 
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Revision as of 12:14, 3 May 2008

File:1v8z.gif

Template:STRUCTURE 1v8z

X-ray crystal structure of the Tryptophan Synthase b2 Subunit from Hyperthermophile, Pyrococcus furiosus


OverviewOverview

The structure of the tryptophan synthase beta2 subunit (Pfbeta2) from the hyperthermophile, Pyrococcus furiosus, was determined by X-ray crystallographic analysis at 2.2 A resolution, and its stability was examined by DSC. This is the first report of the X-ray structure of the tryptophan synthase beta2 subunit alone, although the structure of the tryptophan synthase alpha2beta2 complex from Salmonella typhimurium has already been reported. The structure of Pfbeta2 was essentially similar to that of the beta2 subunit (Stbeta2) in the alpha2beta2 complex from S. typhimurium. The sequence alignment with secondary structures of Pfbeta and Stbeta in monomeric form showed that six residues in the N-terminal region and three residues in the C-terminal region were deleted in Pfbeta, and one residue at Pro366 of Stbeta and at Ile63 of Pfbeta was inserted. The denaturation temperature of Pfbeta2 was higher by 35 degrees C than the reported values from mesophiles at approximately pH 8. On the basis of structural information on both proteins, the analyses of the contributions of each stabilization factor indicate that: (a) the higher stability of Pfbeta2 is not caused by either a hydrophobic interaction or an increase in ion pairs; (b) the number of hydrogen bonds involved in the main chains of Pfbeta is greater by about 10% than that of Stbeta, indicating that the secondary structures of Pfbeta are more stabilized than those of Stbeta and (c) the sequence of Pfbeta seems to be better fitted to an ideally stable structure than that of Stbeta, as assessed from X-ray structure data.

About this StructureAbout this Structure

1V8Z is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of the tryptophan synthase beta subunit from the hyperthermophile Pyrococcus furiosus. Investigation of stabilization factors., Hioki Y, Ogasahara K, Lee SJ, Ma J, Ishida M, Yamagata Y, Matsuura Y, Ota M, Ikeguchi M, Kuramitsu S, Yutani K, Eur J Biochem. 2004 Jul;271(13):2624-35. PMID:15206928 Page seeded by OCA on Sat May 3 12:14:30 2008

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