1tjd: Difference between revisions

Line 1:

[[Image:1tjd.jpg|left|200px]]<br /><applet load="1tjd" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1tjd.jpg|left|200px]]<br /><applet load="1tjd" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1tjd, resolution 2.50Å" />

'''The crystal structure of the reduced disulphide bond isomerase, DsbC, from Escherichia coli'''<br />

==Overview==

Disufide-bond isomerase (DsbC) plays a crucial role in folding, periplasmically excreted bacterial proteins. The crystal structure of the, reduced form of DsbC is presented. The pair of thiol groups from Cys98 and, Cys101 that form the reversible disulfide bond in the enzymatic active, site are 3.1 A apart and the electron density clearly shows that the S, atoms do not form a covalent bond. The other pair of Cys residues (141 and, 163) in DsbC form a disulfide bond. This is different from the previously, reported crystal form of DsbC (McCarthy et al., 2000), in which both Cys, pairs are oxidized. Specific hydrogen-bond interactions are identified, that stabilize the active site in the reactive reduced state with the, special participation of hydrogen bonds between the active-site cysteine, residues (98 and 101) and threonine residues 94 and 182. The present, structure also differs in the orientation of the catalytic domains within, the protein dimer. This is evidence of flexibility within the protein that, probably plays a role in accommodating the substrates in the cleft between, the catalytic domains.

Disufide-bond isomerase (DsbC) plays a crucial role in folding periplasmically excreted bacterial proteins. The crystal structure of the reduced form of DsbC is presented. The pair of thiol groups from Cys98 and Cys101 that form the reversible disulfide bond in the enzymatic active site are 3.1 A apart and the electron density clearly shows that the S atoms do not form a covalent bond. The other pair of Cys residues (141 and 163) in DsbC form a disulfide bond. This is different from the previously reported crystal form of DsbC (McCarthy et al., 2000), in which both Cys pairs are oxidized. Specific hydrogen-bond interactions are identified that stabilize the active site in the reactive reduced state with the special participation of hydrogen bonds between the active-site cysteine residues (98 and 101) and threonine residues 94 and 182. The present structure also differs in the orientation of the catalytic domains within the protein dimer. This is evidence of flexibility within the protein that probably plays a role in accommodating the substrates in the cleft between the catalytic domains.

==About this Structure==

1TJD 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/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TJD OCA].

1TJD 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/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJD OCA].

==Reference==

Line 20:

[[Category: dimer]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 03:19:~~11 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:10 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1tjd.jpg|left|200px]]<br /><applet load="1tjd" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tjd.jpg|left|200px]]<br /><applet load="1tjd" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tjd, resolution 2.50&Aring;" />
 '''The crystal structure of the reduced disulphide bond isomerase, DsbC, from Escherichia coli'''<br />
 ==Overview==
-Disufide-bond isomerase (DsbC) plays a crucial role in folding, periplasmically excreted bacterial proteins. The crystal structure of the, reduced form of DsbC is presented. The pair of thiol groups from Cys98 and, Cys101 that form the reversible disulfide bond in the enzymatic active, site are 3.1 A apart and the electron density clearly shows that the S, atoms do not form a covalent bond. The other pair of Cys residues (141 and, 163) in DsbC form a disulfide bond. This is different from the previously, reported crystal form of DsbC (McCarthy et al., 2000), in which both Cys, pairs are oxidized. Specific hydrogen-bond interactions are identified, that stabilize the active site in the reactive reduced state with the, special participation of hydrogen bonds between the active-site cysteine, residues (98 and 101) and threonine residues 94 and 182. The present, structure also differs in the orientation of the catalytic domains within, the protein dimer. This is evidence of flexibility within the protein that, probably plays a role in accommodating the substrates in the cleft between, the catalytic domains.
+Disufide-bond isomerase (DsbC) plays a crucial role in folding periplasmically excreted bacterial proteins. The crystal structure of the reduced form of DsbC is presented. The pair of thiol groups from Cys98 and Cys101 that form the reversible disulfide bond in the enzymatic active site are 3.1 A apart and the electron density clearly shows that the S atoms do not form a covalent bond. The other pair of Cys residues (141 and 163) in DsbC form a disulfide bond. This is different from the previously reported crystal form of DsbC (McCarthy et al., 2000), in which both Cys pairs are oxidized. Specific hydrogen-bond interactions are identified that stabilize the active site in the reactive reduced state with the special participation of hydrogen bonds between the active-site cysteine residues (98 and 101) and threonine residues 94 and 182. The present structure also differs in the orientation of the catalytic domains within the protein dimer. This is evidence of flexibility within the protein that probably plays a role in accommodating the substrates in the cleft between the catalytic domains.
 ==About this Structure==
-TJD 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/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TJD OCA].
+TJD 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/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJD OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: dimer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:19:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:10 2008''