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4xkk

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Crystal structure of N-terminal domain of Hsp90 from Dictyostelium discoideum

Structural highlights

4xkk is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSC90_DICDI Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).

Publication Abstract from PubMed

Cytosolic heat shock protein 90 (Hsp90) has been implicated in diverse biological processes such as protein folding, cell cycle control, signal transduction, development, and morphological evolution. Model systems available for studying Hsp90 function either allow ease of manipulation for biochemical studies or facilitate a phenomenological study of its role in influencing phenotype. In this work, we have explored the use of the cellular slime mold Dictyostelium discoideum to examine cellular functions of Hsp90 in relation to its multicellular development. In addition to cloning, purification, biochemical characterization, and examination of its crystal structure, our studies, using a pharmacological inhibitor of Hsp90, demonstrate a role for the cytoplasmic isoform (HspD) in D. discoideum development. Inhibition of HspD function using geldanamycin (GA) resulted in delayed aggregation and arrest of D. discoideum development at the 'mound' stage. Crystal structure of the amino-terminal domain of HspD showed a binding pocket similar to that described for yeast Hsp90. Fluorescence spectroscopy, as well as GA-coupled beads affinity pulldown, confirmed a specific interaction between HspD and GA. The results presented here provide an important insight into the function of HspD in D. discoideum development and emphasize the potential of the cellular slime mold to serve as an effective model for studying the many roles of Hsp90 at cellular and organismal levels.

Heat shock protein 90 regulates development in Dictyostelium discoideum.,Sawarkar R, Roy N, Rao S, Raman S, Venketesh S, Suguna K, Tatu U J Mol Biol. 2008 Oct 31;383(1):24-35. doi: 10.1016/j.jmb.2008.08.006. Epub 2008, Aug 7. PMID:18718841^[1]

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

References

↑ Sawarkar R, Roy N, Rao S, Raman S, Venketesh S, Suguna K, Tatu U. Heat shock protein 90 regulates development in Dictyostelium discoideum. J Mol Biol. 2008 Oct 31;383(1):24-35. doi: 10.1016/j.jmb.2008.08.006. Epub 2008, Aug 7. PMID:18718841 doi:http://dx.doi.org/10.1016/j.jmb.2008.08.006

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xkk"

Categories: Dictyostelium discoideum | Large Structures | Raman S | Suguna K

@@ Line 1: / Line 1: @@
 ==Crystal structure of N-terminal domain of Hsp90 from Dictyostelium discoideum==
-<StructureSection load='4xkk' size='340' side='right' caption='[[4xkk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='4xkk' size='340' side='right'caption='[[4xkk]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xkk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XKK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xkk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XKK FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xkk RCSB], [http://www.ebi.ac.uk/pdbsum/4xkk PDBsum]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=4xkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xkk OCA], [https://pdbe.org/4xkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xkk RCSB], [https://www.ebi.ac.uk/pdbsum/4xkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xkk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HSC90_DICDI HSC90_DICDI]] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
+[https://www.uniprot.org/uniprot/HSC90_DICDI HSC90_DICDI] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 15: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xkk" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Raman, S]]
-[[Category: Suguna, K]]
-[[Category: Chaperone]]
 [[Category: Dictyostelium discoideum]]
-[[Category: Hsp90]]
+[[Category: Large Structures]]
+[[Category: Raman S]]
+[[Category: Suguna K]]

4xkk

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Current revision

Crystal structure of N-terminal domain of Hsp90 from Dictyostelium discoideum

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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