This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1uus

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 05:34, 10 October 2019

Structure of an activated Dictyostelium STAT in its DNA-unbound form

Structural highlights

1uus is a 1 chain structure with sequence from Dicdi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1uur
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[STATA_DICDI] Transcription factor that binds to 5'-TTGAATTGA-3' elements in the promoter region of target genes. Functions as repressor of the ecmB gene. Regulates the differentiation of prestalk cells during development.^[1] ^[2] ^[3] ^[4]

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

Dd-STATa is a STAT protein which transcriptionally regulates cellular differentiation in Dictyostelium discoideum, the only non-metazoan known to employ SH2 domain signaling. The 2.7 A crystal structure of a tyrosine phosphorylated Dd-STATa homodimer reveals a four-domain architecture similar to that of mammalian STATs 1 and 3, but with an inverted orientation for the coiled-coil domain. Dimerization is mediated by SH2 domain:phosphopeptide interactions and by a direct interaction between SH2 domains. The unliganded Dd-STATa dimer adopts a fully extended conformation remarkably different from that of the DNA-bound mammalian STATs, implying a large conformational change upon target site recognition. Buried hydrophilic residues predicted to destabilize the coiled-coil domain suggest how hydrophobic residues may become exposed and mediate nuclear export. Functional and evolutionary implications for metazoan STAT proteins are discussed.

Structure of an activated Dictyostelium STAT in its DNA-unbound form.,Soler-Lopez M, Petosa C, Fukuzawa M, Ravelli R, Williams JG, Muller CW Mol Cell. 2004 Mar 26;13(6):791-804. PMID:15053873^[5]

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

References

↑ Mohanty S, Jermyn KA, Early A, Kawata T, Aubry L, Ceccarelli A, Schaap P, Williams JG, Firtel RA. Evidence that the Dictyostelium Dd-STATa protein is a repressor that regulates commitment to stalk cell differentiation and is also required for efficient chemotaxis. Development. 1999 Aug;126(15):3391-405. PMID:10393118
↑ Early A, Gamper M, Moniakis J, Kim E, Hunter T, Williams JG, Firtel RA. Protein tyrosine phosphatase PTP1 negatively regulates Dictyostelium STATa and is required for proper cell-type proportioning. Dev Biol. 2001 Apr 1;232(1):233-45. PMID:11254360 doi:http://dx.doi.org/10.1006/dbio.2001.0171
↑ Soler-Lopez M, Petosa C, Fukuzawa M, Ravelli R, Williams JG, Muller CW. Structure of an activated Dictyostelium STAT in its DNA-unbound form. Mol Cell. 2004 Mar 26;13(6):791-804. PMID:15053873
↑ Kawata T, Shevchenko A, Fukuzawa M, Jermyn KA, Totty NF, Zhukovskaya NV, Sterling AE, Mann M, Williams JG. SH2 signaling in a lower eukaryote: a STAT protein that regulates stalk cell differentiation in dictyostelium. Cell. 1997 Jun 13;89(6):909-16. PMID:9200609
↑ Soler-Lopez M, Petosa C, Fukuzawa M, Ravelli R, Williams JG, Muller CW. Structure of an activated Dictyostelium STAT in its DNA-unbound form. Mol Cell. 2004 Mar 26;13(6):791-804. PMID:15053873

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/1uus"

@@ Line 1: / Line 1: @@
 ==Structure of an activated Dictyostelium STAT in its DNA-unbound form==
-<StructureSection load='1uus' size='340' side='right' caption='[[1uus]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='1uus' size='340' side='right'caption='[[1uus]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1uus]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UUS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1uus]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UUS FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uur|1uur]]</td></tr>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 11735]]
+[[Category: Dicdi]]
+[[Category: Large Structures]]
 [[Category: Fukuzawa, M]]
 [[Category: Muller, C W]]

1uus

From Proteopedia

Revision as of 05:34, 10 October 2019

Structure of an activated Dictyostelium STAT in its DNA-unbound form

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