1prq

From Proteopedia

(Difference between revisions)

Current revision

ACANTHAMOEBA CASTELLANII PROFILIN IA

Structural highlights

1prq is a 1 chain structure with sequence from Acanthamoeba castellanii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRO1A_ACACA Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.

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

Profilin-I from Acanthamoeba castellanii is a 13-kDa protein that binds actin and poly-l-proline. The native protein has been crystallized in two different but closely related forms. The second form proved more amenable to three-dimensional structural determination using heavy-atom isomorphous methods to obtain crystallographic phase information. We used the second crystal structure as a test molecule in the molecular replacement procedure to determine the structure of the first crystal form of profilin-I. More residues participate in crystal lattice contacts in the first crystal form than in the second. The two crystal forms differ significantly in the C-terminal helix that interacts with actin and in the loop preceding this helix. Coordinates of some main chain atoms here differ by about 1.0 A, and side chain atoms differ by more than 2.0 A.

Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii.,Liu S, Fedorov AA, Pollard TD, Lattman EE, Almo SC, Magnus KA J Struct Biol. 1998 Sep;123(1):22-9. PMID:9774541^[1]

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

References

↑ Liu S, Fedorov AA, Pollard TD, Lattman EE, Almo SC, Magnus KA. Crystal packing induces a conformational change in profilin-I from Acanthamoeba castellanii. J Struct Biol. 1998 Sep;123(1):22-9. PMID:9774541 doi:10.1006/jsbi.1998.4009

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1prq' size='340' side='right'caption='[[1prq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1prq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acaca Acaca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1prq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRQ FirstGlance]. <br>
-</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=1prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prq OCA], [https://pdbe.org/1prq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prq RCSB], [https://www.ebi.ac.uk/pdbsum/1prq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prq ProSAT]</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]] 2.5&#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=1prq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prq OCA], [https://pdbe.org/1prq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prq RCSB], [https://www.ebi.ac.uk/pdbsum/1prq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PRO1A_ACACA PRO1A_ACACA]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
+[https://www.uniprot.org/uniprot/PRO1A_ACACA PRO1A_ACACA] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Acaca]]
+[[Category: Acanthamoeba castellanii]]
 [[Category: Large Structures]]
-[[Category: Almo, S C]]
+[[Category: Almo SC]]
-[[Category: Fedorov, A A]]
+[[Category: Fedorov AA]]
-[[Category: Lattman, E E]]
+[[Category: Lattman EE]]
-[[Category: Pollard, T D]]
+[[Category: Pollard TD]]
-[[Category: Way, M]]
+[[Category: Way M]]
-[[Category: Actin-binding protein]]
-[[Category: Contractile protein]]

1prq

From Proteopedia

Current revision

ACANTHAMOEBA CASTELLANII PROFILIN IA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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