1b89: Difference between revisions

Revision as of 03:21, 7 August 2014

CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)

Structural highlights

1b89 is a 1 chain structure with sequence from Bos taurus. The April 2007 RCSB PDB Molecule of the Month feature on Clathrin by Graham T. Johnson and David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	MSE
Resources:	FirstGlance, OCA, RCSB, PDBsum

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

Clathrin is a triskelion-shaped cytoplasmic protein that polymerizes into a polyhedral lattice on intracellular membranes to form protein-coated membrane vesicles. Lattice formation induces the sorting of membrane proteins during endocytosis and organelle biogenesis by interacting with membrane-associated adaptor molecules. The clathrin triskelion is a trimer of heavy-chain subunits (1,675 residues), each binding a single light-chain subunit, in the hub domain (residues 1,074-1,675). Light chains negatively modulate polymerization so that intracellular clathrin assembly is adaptor-dependent. Here we report the atomic structure, to 2.6 A resolution, of hub residues 1,210-1,516 involved in mediating spontaneous clathrin heavy-chain polymerization and light-chain association. The hub fragment folds into an elongated coil of alpha-helices, and alignment analyses reveal a 145-residue motif that is repeated seven times along the filamentous leg and appears in other proteins involved in vacuolar protein sorting. The resulting model provides a three-dimensional framework for understanding clathrin heavy-chain self-assembly, light-chain binding and trimerization.

Clathrin self-assembly is mediated by a tandemly repeated superhelix.,Ybe JA, Brodsky FM, Hofmann K, Lin K, Liu SH, Chen L, Earnest TN, Fletterick RJ, Hwang PK Nature. 1999 May 27;399(6734):371-5. PMID:10360576^[1]

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

References

↑ Ybe JA, Brodsky FM, Hofmann K, Lin K, Liu SH, Chen L, Earnest TN, Fletterick RJ, Hwang PK. Clathrin self-assembly is mediated by a tandemly repeated superhelix. Nature. 1999 May 27;399(6734):371-5. PMID:10360576 doi:https://dx.doi.org/10.1038/20708

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Ybe JA, Brodsky FM, Hofmann K, Lin K, Liu SH, Chen L, Earnest TN, Fletterick RJ, Hwang PK. Clathrin self-assembly is mediated by a tandemly repeated superhelix. Nature. 1999 May 27;399(6734):371-5. PMID:10360576 doi:https://dx.doi.org/10.1038/20708

[1]

@@ Line 1: / Line 1: @@
-[[Image:1b89.png|left|200px]]
+==CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)==
+<StructureSection load='1b89' size='340' side='right' caption='[[1b89]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1b89]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The April 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Clathrin''  by Graham T. Johnson and David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_4 10.2210/rcsb_pdb/mom_2007_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B89 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B89 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b89 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b89 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b89 RCSB], [http://www.ebi.ac.uk/pdbsum/1b89 PDBsum]</span></td></tr>
+<table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b8/1b89_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Clathrin is a triskelion-shaped cytoplasmic protein that polymerizes into a polyhedral lattice on intracellular membranes to form protein-coated membrane vesicles. Lattice formation induces the sorting of membrane proteins during endocytosis and organelle biogenesis by interacting with membrane-associated adaptor molecules. The clathrin triskelion is a trimer of heavy-chain subunits (1,675 residues), each binding a single light-chain subunit, in the hub domain (residues 1,074-1,675). Light chains negatively modulate polymerization so that intracellular clathrin assembly is adaptor-dependent. Here we report the atomic structure, to 2.6 A resolution, of hub residues 1,210-1,516 involved in mediating spontaneous clathrin heavy-chain polymerization and light-chain association. The hub fragment folds into an elongated coil of alpha-helices, and alignment analyses reveal a 145-residue motif that is repeated seven times along the filamentous leg and appears in other proteins involved in vacuolar protein sorting. The resulting model provides a three-dimensional framework for understanding clathrin heavy-chain self-assembly, light-chain binding and trimerization.
-{{STRUCTURE_1b89|  PDB=1b89  |  SCENE=  }}
+Clathrin self-assembly is mediated by a tandemly repeated superhelix.,Ybe JA, Brodsky FM, Hofmann K, Lin K, Liu SH, Chen L, Earnest TN, Fletterick RJ, Hwang PK Nature. 1999 May 27;399(6734):371-5. PMID:10360576<ref>PMID:10360576</ref>
-===CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_10360576}}
-==About this Structure==
-[[1b89]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The April 2007 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Clathrin''  by Graham T. Johnson and David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2007_4 10.2210/rcsb_pdb/mom_2007_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B89 OCA].
 ==See Also==
 *[[Clathrin|Clathrin]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:010360576</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
 [[Category: Clathrin]]

1b89: Difference between revisions

Revision as of 03:21, 7 August 2014

CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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