2ykt

From Proteopedia

(Difference between revisions)

Revision as of 07:29, 1 April 2015

Crystal structure of the I-BAR domain of IRSp53 (BAIAP2) in complex with an EHEC derived Tir peptide

Structural highlights

2ykt is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1wdz, 1y2o
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[BAIP2_HUMAN] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.^[1] ^[2] ^[3] ^[4] [TIR_ECO5T] Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion (By similarity).

Publication Abstract from PubMed

Actin assembly beneath enterohemorrhagic E. coli (EHEC) attached to its host cell is triggered by the intracellular interaction of its translocated effector proteins Tir and EspF(U) with human IRSp53 family proteins and N-WASP. Here, we report the structure of the N-terminal I-BAR domain of IRSp53 in complex with a Tir-derived peptide, in which the homodimeric I-BAR domain binds two Tir molecules aligned in parallel. This arrangement provides a protein scaffold linking the bacterium to the host cell's actin polymerization machinery. The structure uncovers a specific peptide-binding site on the I-BAR surface, conserved between IRSp53 and IRTKS. The Tir Asn-Pro-Tyr (NPY) motif, essential for pedestal formation, is specifically recognized by this binding site. The site was confirmed by mutagenesis and in vivo-binding assays. It is possible that IRSp53 utilizes the NPY-binding site for additional interactions with as yet unknown partners within the host cell.

Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli.,de Groot JC, Schluter K, Carius Y, Quedenau C, Vingadassalom D, Faix J, Weiss SM, Reichelt J, Standfuss-Gabisch C, Lesser CF, Leong JM, Heinz DW, Bussow K, Stradal TE Structure. 2011 Sep 7;19(9):1294-306. PMID:21893288^[5]

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

References

↑ Miki H, Yamaguchi H, Suetsugu S, Takenawa T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. PMID:11130076 doi:http://dx.doi.org/10.1038/35047107
↑ Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A. Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. Curr Biol. 2001 Oct 30;11(21):1645-55. PMID:11696321
↑ Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N. A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J Biol Chem. 2004 Apr 9;279(15):14929-36. Epub 2004 Jan 29. PMID:14752106 doi:http://dx.doi.org/10.1074/jbc.M309408200
↑ Vingadassalom D, Kazlauskas A, Skehan B, Cheng HC, Magoun L, Robbins D, Rosen MK, Saksela K, Leong JM. Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation. Proc Natl Acad Sci U S A. 2009 Apr 21;106(16):6754-9. doi:, 10.1073/pnas.0809131106. Epub 2009 Apr 6. PMID:19366662 doi:10.1073/pnas.0809131106
↑ de Groot JC, Schluter K, Carius Y, Quedenau C, Vingadassalom D, Faix J, Weiss SM, Reichelt J, Standfuss-Gabisch C, Lesser CF, Leong JM, Heinz DW, Bussow K, Stradal TE. Structural basis for complex formation between human IRSp53 and the translocated intimin receptor Tir of enterohemorrhagic E. coli. Structure. 2011 Sep 7;19(9):1294-306. PMID:21893288 doi:10.1016/j.str.2011.06.015

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ykt"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE I-BAR DOMAIN OF IRSP53 (BAIAP2) IN COMPLEX WITH AN EHEC DERIVED TIR PEPTIDE==
+==Crystal structure of the I-BAR domain of IRSp53 (BAIAP2) in complex with an EHEC derived Tir peptide==
 <StructureSection load='2ykt' size='340' side='right' caption='[[2ykt]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ykt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ykt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKT FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref>  [[http://www.uniprot.org/uniprot/C6UYL8_ECO5T C6UYL8_ECO5T]] Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion (By similarity).
+[[http://www.uniprot.org/uniprot/BAIP2_HUMAN BAIP2_HUMAN]] Adapter protein that links membrane-bound small G-proteins to cytoplasmic effector proteins. Necessary for CDC42-mediated reorganization of the actin cytoskeleton and for RAC1-mediated membrane ruffling. Involved in the regulation of the actin cytoskeleton by WASF family members and the Arp2/3 complex. Plays a role in neurite growth. Acts syngeristically with ENAH to promote filipodia formation. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.<ref>PMID:11130076</ref> <ref>PMID:11696321</ref> <ref>PMID:14752106</ref> <ref>PMID:19366662</ref>  [[http://www.uniprot.org/uniprot/TIR_ECO5T TIR_ECO5T]] Multifunctional protein that is required for efficient pedestal formation in host epithelial cells during infection. The extracellular region acts as a receptor for bacterial intimin, allowing the bacterium to attach tightly to the host-cell surface. Simultaneously, the intracellular region initiates a signaling cascade in the host cell, which leads to actin polymerization and formation of actin pedestals at the sites of bacterial adhesion (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Buessow, K]]
 [[Category: Carius, Y]]
 [[Category: Faix, J]]
-[[Category: Groot, J C.De]]
+[[Category: Groot, J C.de]]
 [[Category: Heinz, D W]]
 [[Category: Leong, J M]]

2ykt

From Proteopedia

Revision as of 07:29, 1 April 2015

Crystal structure of the I-BAR domain of IRSp53 (BAIAP2) in complex with an EHEC derived Tir peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox