2bjx
From Proteopedia
(New page: 200px<br /> <applet load="2bjx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bjx" /> '''PROTEIN DISULFIDE ISOMERASE'''<br /> ==Ove...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2bjx. | + | [[Image:2bjx.jpg|left|200px]]<br /><applet load="2bjx" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bjx" size=" | + | |
caption="2bjx" /> | caption="2bjx" /> | ||
'''PROTEIN DISULFIDE ISOMERASE'''<br /> | '''PROTEIN DISULFIDE ISOMERASE'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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:// | + | 2BJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=2BJX OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 26: | ||
[[Category: redox-active center]] | [[Category: redox-active center]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:16:22 2008'' |
Revision as of 15:16, 15 February 2008
|
PROTEIN DISULFIDE ISOMERASE
Overview
Protein disulfide isomerase (PDI) is a multifunctional protein of the, endoplasmic reticulum, which catalyzes the formation, breakage and, rearrangement of disulfide bonds during protein folding. It consists of, four domains designated a, b, b and a. Both a and a domains contains an, active site with the sequence motif -Cys-Gly-His-Cys-involved directly in, thiol-disulfide exchange reactions. As expected these domains have, structures very similar to the ubiquitous redox protein thioredoxin. A, low-resolution NMR structure of the b domain revealed that this domain, adopts a fold similar to the PDI a domain and thioredoxin [Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M. and Creighton, T.E. (1997) Curr., Biol. 7, 239-245]. A refined ensemble of solution structures based on the, input of 1865 structural restraints shows that the structure of PDI b is, well defined throughout the complete protein except for about 10 residues, at the C-terminus of the sequence. 15N relaxation data show that these, residues are disordered and not part of this structural domain. Therefore, the domain boundaries of PDI can now be fixed with reasonable precision., Structural comparison of the PDI b domain with thioredoxin and PDI a, reveals several features important for thiol-disulfide exchange activity.
About this Structure
2BJX is a Single protein structure of sequence from Homo sapiens. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.
Reference
The structure in solution of the b domain of protein disulfide isomerase., Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ, J Biomol NMR. 1999 Apr;13(4):357-68. PMID:10383197
Page seeded by OCA on Fri Feb 15 17:16:22 2008
