This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1wkv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wkv.gif|left|200px]]<br /><applet load="1wkv" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1wkv.gif|left|200px]]
-
caption="1wkv, resolution 2.0&Aring;" />
+
 
-
'''Crystal structure of O-phosphoserine sulfhydrylase'''<br />
+
{{Structure
 +
|PDB= 1wkv |SIZE=350|CAPTION= <scene name='initialview01'>1wkv</scene>, resolution 2.0&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
 +
|ACTIVITY=
 +
|GENE= APE1586 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56636 Aeropyrum pernix])
 +
}}
 +
 
 +
'''Crystal structure of O-phosphoserine sulfhydrylase'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1WKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKV OCA].
+
1WKV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKV OCA].
==Reference==
==Reference==
-
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution., Oda Y, Mino K, Ishikawa K, Ataka M, J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16005886 16005886]
+
Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution., Oda Y, Mino K, Ishikawa K, Ataka M, J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16005886 16005886]
[[Category: Aeropyrum pernix]]
[[Category: Aeropyrum pernix]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 22: Line 31:
[[Category: open alpha/beta folding]]
[[Category: open alpha/beta folding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:27 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:58:15 2008''

Revision as of 12:58, 20 March 2008

Image:1wkv.gif


PDB ID 1wkv

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: and
Gene: APE1586 (Aeropyrum pernix)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of O-phosphoserine sulfhydrylase


Overview

O-Phosphoserine sulfhydrylase is a new enzyme found in a hyperthermophilic archaeon, Aeropyrum pernix K1. This enzyme catalyzes a novel cysteine synthetic reaction from O-phospho-l-serine and sulfide. The crystal structure of the enzyme was determined at 2.0A resolution using the method of multi-wavelength anomalous dispersion. A monomer consists of three domains, including an N-terminal domain with a new alpha/beta fold. The topology folds of the middle and C-terminal domains were similar to those of the O-acetylserine sulfhydrylase-A from Salmonella typhimurium and the cystathionine beta-synthase from human. The cofactor, pyridoxal 5'-phosphate, is bound in a cleft between the middle and C-terminal domains through a covalent linkage to Lys127. Based on the structure determined, O-phospho-l-serine could be rationally modeled into the active site of the enzyme. An enzyme-substrate complex model and a mutation experiment revealed that Arg297, unique to hyperthermophilic archaea, is one of the most crucial residues for O-phosphoserine sulfhydrylation activity. There are more hydrophobic areas and less electric charges at the dimer interface, compared to the S.typhimurium O-acetylserine sulfhydrylase.

About this Structure

1WKV is a Single protein structure of sequence from Aeropyrum pernix. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution., Oda Y, Mino K, Ishikawa K, Ataka M, J Mol Biol. 2005 Aug 12;351(2):334-44. PMID:16005886

Page seeded by OCA on Thu Mar 20 14:58:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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