1n57: Difference between revisions

Revision as of 15:02, 21 February 2008

Crystal Structure of Chaperone Hsp31

OverviewOverview

Heat shock proteins (Hsps) play essential protective roles under stress conditions by preventing the formation of protein aggregates and degrading misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a representative member of a family of chaperones that alleviates protein misfolding by interacting with early unfolding intermediates. The 1.6-A crystal structure of the EcHsp31 dimer reveals a system of hydrophobic patches, canyons, and grooves, which may stabilize partially unfolded substrate. The presence of a well conserved, yet buried, triad in each two-domain subunit suggests a still unproven hydrolytic function of the protein. A flexible extended linker between the A and P domains may play a role in conformational flexibility and substrate binding. The alpha-beta sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a protease belonging to the DJ-1 superfamily. The structure-guided sequence alignment indicates that Hsp31 homologs can be divided in three classes based on variations in the P domain that dramatically affect both oligomerization and catalytic triad formation.

About this StructureAbout this Structure

1N57 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad., Quigley PM, Korotkov K, Baneyx F, Hol WG, Proc Natl Acad Sci U S A. 2003 Mar 18;100(6):3137-42. Epub 2003 Mar 5. PMID:12621151

Page seeded by OCA on Thu Feb 21 14:02:23 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1n57.gif|left|200px]]<br /><applet load="1n57" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1n57.gif|left|200px]]<br /><applet load="1n57" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1n57, resolution 1.6&Aring;" />
 '''Crystal Structure of Chaperone Hsp31'''<br />
 ==Overview==
-Heat shock proteins (Hsps) play essential protective roles under stress, conditions by preventing the formation of protein aggregates and degrading, misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a, representative member of a family of chaperones that alleviates protein, misfolding by interacting with early unfolding intermediates. The 1.6-A, crystal structure of the EcHsp31 dimer reveals a system of hydrophobic, patches, canyons, and grooves, which may stabilize partially unfolded, substrate. The presence of a well conserved, yet buried, triad in each, two-domain subunit suggests a still unproven hydrolytic function of the, protein. A flexible extended linker between the A and P domains may play a, role in conformational flexibility and substrate binding. The alpha-beta, sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a, protease belonging to the DJ-1 superfamily. The structure-guided sequence, alignment indicates that Hsp31 homologs can be divided in three classes, based on variations in the P domain that dramatically affect both, oligomerization and catalytic triad formation.
+Heat shock proteins (Hsps) play essential protective roles under stress conditions by preventing the formation of protein aggregates and degrading misfolded proteins. EcHsp31, the yedU (hchA) gene product, is a representative member of a family of chaperones that alleviates protein misfolding by interacting with early unfolding intermediates. The 1.6-A crystal structure of the EcHsp31 dimer reveals a system of hydrophobic patches, canyons, and grooves, which may stabilize partially unfolded substrate. The presence of a well conserved, yet buried, triad in each two-domain subunit suggests a still unproven hydrolytic function of the protein. A flexible extended linker between the A and P domains may play a role in conformational flexibility and substrate binding. The alpha-beta sandwich of the EcHsp31 monomer shows structural similarity to PhPI, a protease belonging to the DJ-1 superfamily. The structure-guided sequence alignment indicates that Hsp31 homologs can be divided in three classes based on variations in the P domain that dramatically affect both oligomerization and catalytic triad formation.
 ==About this Structure==
-N57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N57 OCA].
+N57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N57 OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Baneyx, F.]]
-[[Category: Hol, W.G.J.]]
+[[Category: Hol, W G.J.]]
 [[Category: Korotkov, K.]]
-[[Category: Quigley, P.M.]]
+[[Category: Quigley, P M.]]
 [[Category: MG]]
 [[Category: alpha-beta sandwich]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:58:18 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:23 2008''