2pv2: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2pv2.jpg|left|200px]]<br /><applet load="2pv2" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:2pv2.jpg|left|200px]]
-caption="2pv2, resolution 1.300&Aring;" />
-'''Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK'''<br />
+ {{Structure
+|PDB= 2pv2 |SIZE=350|CAPTION= <scene name='initialview01'>2pv2</scene>, resolution 1.300&Aring;
+|SITE=
+|LIGAND=
+|ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8]
+|GENE= surA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+}}
+'''Crystallographic Structure of SurA first peptidyl-prolyl isomerase domain complexed with peptide NFTLKFWDIFRK'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-PV2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PV2 OCA].
+PV2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PV2 OCA].
 ==Reference==
-The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues., Xu X, Wang S, Hu YX, McKay DB, J Mol Biol. 2007 Oct 19;373(2):367-81. Epub 2007 Aug 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17825319 17825319]
+The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues., Xu X, Wang S, Hu YX, McKay DB, J Mol Biol. 2007 Oct 19;373(2):367-81. Epub 2007 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17825319 17825319]
 [[Category: Escherichia coli]]
 [[Category: Peptidylprolyl isomerase]]
@@ Line 18: / Line 27: @@
 [[Category: peptide]]
 [[Category: peptidyl-prolyl cis-trans isomerase domain]]
-[[Category: survival protein a]]
+[[Category: survival protein some]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:33:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:17:45 2008''