1bjx

From Proteopedia

(Difference between revisions)

Current revision

HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES

Structural highlights

1bjx is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDIA1_HUMAN This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mezghrani A, Courageot J, Mani JC, Pugniere M, Bastiani P, Miquelis R. Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent thyroglobulin/PDI interactions determine a novel PDI function in the post-endoplasmic reticulum of thyrocytes. J Biol Chem. 2000 Jan 21;275(3):1920-9. PMID:10636893
↑ Lumb RA, Bulleid NJ. Is protein disulfide isomerase a redox-dependent molecular chaperone? EMBO J. 2002 Dec 16;21(24):6763-70. PMID:12485997
↑ Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ. The structure in solution of the b domain of protein disulfide isomerase. J Biomol NMR. 1999 Apr;13(4):357-68. PMID:10383197

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bjx"

@@ Line 1: / Line 1: @@
-[[Image:1bjx.gif|left|200px]]<br />
-<applet load="1bjx" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1bjx" />
-'''HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES'''<br />
-==Overview==
+==HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES==
-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.
+<StructureSection load='1bjx' size='340' side='right'caption='[[1bjx]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1bjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BJX FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjx OCA], [https://pdbe.org/1bjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bjx RCSB], [https://www.ebi.ac.uk/pdbsum/1bjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bj/1bjx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bjx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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<ref>PMID:10383197</ref>
-BJX 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BJX OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10383197 10383197]
+</div>
+<div class="pdbe-citations 1bjx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein disulfide-isomerase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Darby NJ]]
-[[Category: Darby, N.J.]]
+[[Category: Dijkstra K]]
-[[Category: Dijkstra, K.]]
+[[Category: Kemmink J]]
-[[Category: Kemmink, J.]]
+[[Category: Mariani M]]
-[[Category: Mariani, M.]]
+[[Category: Nilges M]]
-[[Category: Nilges, M.]]
+[[Category: Penka E]]
-[[Category: Penka, E.]]
+[[Category: Scheek RM]]
-[[Category: Scheek, R.M.]]
-[[Category: electron transport]]
-[[Category: endoplasmic reticulum]]
-[[Category: isomerase]]
-[[Category: redox-active center]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:10:51 2007''

1bjx

From Proteopedia

Current revision

HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox