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.

2rjw

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:51, 5 September 2018

The crystal structure of the H41Y mutant of villin headpiece, P61 SPACE GROUP.

Structural highlights

2rjw is a 2 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1yu5, 1yu7, 1yu8, 2rjv, 2rjx, 2rjy
Gene:	VIL1, VIL (CHICK)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VILI_CHICK] Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair (By similarity). Its actin-bundling activity is inhibited by tropomyosin.^[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

The villin headpiece domain (HP67) is the C-terminal F-actin-binding motif that confers F-actin-bundling activity to villin, a component of the actin bundles that support the brush-border microvilli. It has been investigated extensively by both experimental and theoretical measurements. Our laboratory, for example, has determined both its NMR and its crystal structures. This study presents the structures of HP67 and its pH-stabilized mutant (H41Y) in a different crystal form and space group. For both constructs, two molecules are found in each asymmetric unit in the new space group P6(1). While one of the two structures (Mol A) is structurally similar to our previously determined structure (Mol X), the other (Mol B) has significant deviations, especially in the N-terminal subdomain, where lattice contacts do not appear to contribute to the difference. In addition, the structurally most different crystal structure, Mol B, is actually closer to the averaged NMR structure. Harmonic motions, as suggested by the B-factor profiles, differ between these crystal structures; crystal structures from the same space group share a similar pattern. Thus, heterogeneity and dynamics are observed in different crystal structures of the same protein even for a protein as small as villin headpiece.

Heterogeneity and dynamics in villin headpiece crystal structures.,Meng J, McKnight CJ Acta Crystallogr D Biol Crystallogr. 2009 May;65(Pt 5):470-6. Epub 2009, Apr 18. PMID:19390152^[3]

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

References

↑ Burgess DR, Broschat KO, Hayden JM. Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins. J Cell Biol. 1987 Jan;104(1):29-40. PMID:3793760
↑ de Arruda MV, Bazari H, Wallek M, Matsudaira P. An actin footprint on villin. Single site substitutions in a cluster of basic residues inhibit the actin severing but not capping activity of villin. J Biol Chem. 1992 Jun 25;267(18):13079-85. PMID:1618806
↑ Meng J, McKnight CJ. Heterogeneity and dynamics in villin headpiece crystal structures. Acta Crystallogr D Biol Crystallogr. 2009 May;65(Pt 5):470-6. Epub 2009, Apr 18. PMID:19390152 doi:10.1107/S0907444909008646

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/2rjw"

@@ Line 1: / Line 1: @@
 ==The crystal structure of the H41Y mutant of villin headpiece, P61 SPACE GROUP.==
 <StructureSection load='2rjw' size='340' side='right' caption='[[2rjw]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yu5|1yu5]], [[1yu7|1yu7]], [[1yu8|1yu8]], [[2rjv|2rjv]], [[2rjx|2rjx]], [[2rjy|2rjy]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIL1, VIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=2rjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjw OCA], [http://pdbe.org/2rjw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rjw RCSB], [http://www.ebi.ac.uk/pdbsum/2rjw PDBsum]</span></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=2rjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjw OCA], [http://pdbe.org/2rjw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rjw RCSB], [http://www.ebi.ac.uk/pdbsum/2rjw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjw ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 40: / Line 41: @@
 [[Category: Actin capping]]
 [[Category: Actin-binding]]
+[[Category: Calcium]]
+[[Category: Cytoplasm]]
 [[Category: Cytoskeleton]]
 [[Category: Helix]]
 [[Category: Structural protein]]

2rjw

From Proteopedia

Revision as of 10:51, 5 September 2018

The crystal structure of the H41Y mutant of villin headpiece, P61 SPACE GROUP.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox