3lju: Difference between revisions

Latest revision as of 08:38, 6 September 2023

Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3

Structural highlights

3lju is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.702Å
Ligands:	IP9, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADAP1_HUMAN GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4).^[1] ^[2]

Publication Abstract from PubMed

Phosphatidylinositol 3,4,5-triphosphate (PIP3) plays a key role in neuronal polarization and axon formation. PIP3-containing vesicles are transported to axon tips by the kinesin KIF13B via an adaptor protein, centaurin alpha1 (CENTA1). KIF13B interacts with CENTA1 through its forkhead-associated (FHA) domain. We solved the crystal structures of CENTA1 in ligand-free, KIF13B-FHA domain-bound, and PIP3 head group (IP4)-bound conformations, and the CENTA1/KIF13B-FHA/IP4 ternary complex. The first pleckstrin homology (PH) domain of CENTA1 specifically binds to PIP3, while the second binds to both PIP3 and phosphatidylinositol 3,4-biphosphate (PI(3,4)P(2)). The FHA domain of KIF13B interacts with the PH1 domain of one CENTA1 molecule and the ArfGAP domain of a second CENTA1 molecule in a threonine phosphorylation-independent fashion. We propose that full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule.

Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1.,Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, Mackenzie F, Chishti AH, Park HW Proc Natl Acad Sci U S A. 2010 Nov 5. PMID:21057110^[3]

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

References

↑ Venkateswarlu K, Cullen PJ. Molecular cloning and functional characterization of a human homologue of centaurin-alpha. Biochem Biophys Res Commun. 1999 Aug 19;262(1):237-44. PMID:10448098 doi:10.1006/bbrc.1999.1065
↑ Venkateswarlu K, Oatey PB, Tavare JM, Jackson TR, Cullen PJ. Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1. Biochem J. 1999 Jun 1;340 ( Pt 2):359-63. PMID:10333475
↑ Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, Mackenzie F, Chishti AH, Park HW. Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1. Proc Natl Acad Sci U S A. 2010 Nov 5. PMID:21057110 doi:10.1073/pnas.1009008107

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Venkateswarlu K, Cullen PJ. Molecular cloning and functional characterization of a human homologue of centaurin-alpha. Biochem Biophys Res Commun. 1999 Aug 19;262(1):237-44. PMID:10448098 doi:10.1006/bbrc.1999.1065

[2] Venkateswarlu K, Oatey PB, Tavare JM, Jackson TR, Cullen PJ. Identification of centaurin-alpha1 as a potential in vivo phosphatidylinositol 3,4,5-trisphosphate-binding protein that is functionally homologous to the yeast ADP-ribosylation factor (ARF) GTPase-activating protein, Gcs1. Biochem J. 1999 Jun 1;340 ( Pt 2):359-63. PMID:10333475

[3] Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, Mackenzie F, Chishti AH, Park HW. Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1. Proc Natl Acad Sci U S A. 2010 Nov 5. PMID:21057110 doi:10.1073/pnas.1009008107

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3lju.png|left|200px]]
-<!--
+==Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3==
-The line below this paragraph, containing "STRUCTURE_3lju", creates the "Structure Box" on the page.
+<StructureSection load='3lju' size='340' side='right'caption='[[3lju]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3lju]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LJU FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.702&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IP9:(2R)-3-{[(R)-{[(1S,2S,3R,4S,5S,6S)-2,6-DIHYDROXY-3,4,5-TRIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}(HYDROXY)PHOSPHORYL]OXY}PROPANE-1,2-DIYL+DIOCTANOATE'>IP9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_3lju|  PDB=3lju  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lju OCA], [https://pdbe.org/3lju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lju RCSB], [https://www.ebi.ac.uk/pdbsum/3lju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lju ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ADAP1_HUMAN ADAP1_HUMAN] GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4).<ref>PMID:10448098</ref> <ref>PMID:10333475</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Phosphatidylinositol 3,4,5-triphosphate (PIP3) plays a key role in neuronal polarization and axon formation. PIP3-containing vesicles are transported to axon tips by the kinesin KIF13B via an adaptor protein, centaurin alpha1 (CENTA1). KIF13B interacts with CENTA1 through its forkhead-associated (FHA) domain. We solved the crystal structures of CENTA1 in ligand-free, KIF13B-FHA domain-bound, and PIP3 head group (IP4)-bound conformations, and the CENTA1/KIF13B-FHA/IP4 ternary complex. The first pleckstrin homology (PH) domain of CENTA1 specifically binds to PIP3, while the second binds to both PIP3 and phosphatidylinositol 3,4-biphosphate (PI(3,4)P(2)). The FHA domain of KIF13B interacts with the PH1 domain of one CENTA1 molecule and the ArfGAP domain of a second CENTA1 molecule in a threonine phosphorylation-independent fashion. We propose that full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule.
-===Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3===
+Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin {alpha}1.,Tong Y, Tempel W, Wang H, Yamada K, Shen L, Senisterra GA, Mackenzie F, Chishti AH, Park HW Proc Natl Acad Sci U S A. 2010 Nov 5. PMID:21057110<ref>PMID:21057110</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_21057110}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3lju" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21057110 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21057110}}
+__TOC__
+</StructureSection>
-==About this Structure==
-LJU is a 1 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=3LJU OCA].
-==Reference==
-<ref group="xtra">PMID:21057110</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H.]]
+[[Category: Large Structures]]
-[[Category: Bochkarev, A.]]
+[[Category: Arrowsmith CH]]
-[[Category: Bountra, C.]]
+[[Category: Bochkarev A]]
-[[Category: Edwards, A M.]]
+[[Category: Bountra C]]
-[[Category: MacKenzie, F.]]
+[[Category: Edwards AM]]
-[[Category: Park, H.]]
+[[Category: MacKenzie F]]
-[[Category: SGC, Structural Genomics Consortium.]]
+[[Category: Park H]]
-[[Category: Shen, L.]]
+[[Category: Shen L]]
-[[Category: Tempel, W.]]
+[[Category: Tempel W]]
-[[Category: Tong, Y.]]
+[[Category: Tong Y]]
-[[Category: Weigelt, J.]]
+[[Category: Weigelt J]]
-[[Category: Gap]]
-[[Category: Gtpase activation]]
-[[Category: Hydrolase activator]]
-[[Category: Metal-binding]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Sgc]]
-[[Category: Structural genomics consortium]]
-[[Category: Zinc-finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:15:05 2010''

3lju: Difference between revisions

Latest revision as of 08:38, 6 September 2023

Crystal structure of full length centaurin alpha-1 bound with the head group of PIP3

Structural highlights

Function

Publication Abstract from PubMed

References

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