1js1
From Proteopedia
(New page: 200px<br /><applet load="1js1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1js1, resolution 2.00Å" /> '''Crystal Structure of...) |
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| - | [[Image:1js1.gif|left|200px]]<br /><applet load="1js1" size=" | + | [[Image:1js1.gif|left|200px]]<br /><applet load="1js1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1js1, resolution 2.00Å" /> | caption="1js1, resolution 2.00Å" /> | ||
'''Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution'''<br /> | '''Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A transcarbamylase-like protein essential for arginine biosynthesis in the | + | A transcarbamylase-like protein essential for arginine biosynthesis in the anaerobic bacterium Bacteroides fragilis has been purified and crystallized in space group P4(3)2(1)2 (a=b=153.4 A, c=94.8 A). The structure was solved using a single isomorphous replacement with anomalous scattering (SIRAS) and was refined at 2.0 A resolution to an R-factor of 20.6% (R-free=25.2%). The molecular model is trimeric and comprises 960 amino acid residues, two phosphate groups and 422 water molecules. The monomer has the consensus transcarbamylase fold with two structural domains linked by two long interdomain helices: the putative carbamoyl phosphate-binding domain and a binding domain for the second substrate. Each domain has a central parallel beta-sheet surrounded by alpha-helices and loops with alpha/beta topology. The putative carbamoyl phosphate-binding site is similar to those in ornithine transcarbamylases (OTCases) and aspartate transcarbamylases (ATCases); however, the second substrate-binding site is strikingly different. This site has several insertions and deletions, and residues critical to substrate binding and catalysis in other known transcarbamylases are not conserved. The three-dimensional structure and the fact that this protein is essential for arginine biosynthesis suggest strongly that it is a new member of the transcarbamylase family. A similar protein has been found in Xylella fastidiosa, a bacterium that infects grapes, citrus and other plants. |
==About this Structure== | ==About this Structure== | ||
| - | 1JS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JS1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacteroides fragilis]] | [[Category: Bacteroides fragilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Allewell, N | + | [[Category: Allewell, N M.]] |
[[Category: Gallegos, R.]] | [[Category: Gallegos, R.]] | ||
| - | [[Category: III, J | + | [[Category: III, J DePonte.]] |
[[Category: Malamy, M.]] | [[Category: Malamy, M.]] | ||
[[Category: Morizono, H.]] | [[Category: Morizono, H.]] | ||
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[[Category: two domains]] | [[Category: two domains]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:06 2008'' |
Revision as of 11:26, 21 February 2008
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Crystal Structure of a new transcarbamylase from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution
Overview
A transcarbamylase-like protein essential for arginine biosynthesis in the anaerobic bacterium Bacteroides fragilis has been purified and crystallized in space group P4(3)2(1)2 (a=b=153.4 A, c=94.8 A). The structure was solved using a single isomorphous replacement with anomalous scattering (SIRAS) and was refined at 2.0 A resolution to an R-factor of 20.6% (R-free=25.2%). The molecular model is trimeric and comprises 960 amino acid residues, two phosphate groups and 422 water molecules. The monomer has the consensus transcarbamylase fold with two structural domains linked by two long interdomain helices: the putative carbamoyl phosphate-binding domain and a binding domain for the second substrate. Each domain has a central parallel beta-sheet surrounded by alpha-helices and loops with alpha/beta topology. The putative carbamoyl phosphate-binding site is similar to those in ornithine transcarbamylases (OTCases) and aspartate transcarbamylases (ATCases); however, the second substrate-binding site is strikingly different. This site has several insertions and deletions, and residues critical to substrate binding and catalysis in other known transcarbamylases are not conserved. The three-dimensional structure and the fact that this protein is essential for arginine biosynthesis suggest strongly that it is a new member of the transcarbamylase family. A similar protein has been found in Xylella fastidiosa, a bacterium that infects grapes, citrus and other plants.
About this Structure
1JS1 is a Single protein structure of sequence from Bacteroides fragilis with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a transcarbamylase-like protein from the anaerobic bacterium Bacteroides fragilis at 2.0 A resolution., Shi D, Gallegos R, DePonte J 3rd, Morizono H, Yu X, Allewell NM, Malamy M, Tuchman M, J Mol Biol. 2002 Jul 19;320(4):899-908. PMID:12095263
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