2a28: Difference between revisions

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<StructureSection load='2a28' size='340' side='right'caption='[[2a28]], [[Resolution|resolution]] 1.07&Aring;' scene=''>
<StructureSection load='2a28' size='340' side='right'caption='[[2a28]], [[Resolution|resolution]] 1.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2a28]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A28 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2a28]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A28 FirstGlance]. <br>
</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=2a28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a28 OCA], [http://pdbe.org/2a28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a28 RCSB], [http://www.ebi.ac.uk/pdbsum/2a28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a28 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]] 1.07&#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=2a28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a28 OCA], [https://pdbe.org/2a28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a28 RCSB], [https://www.ebi.ac.uk/pdbsum/2a28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a28 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/BZZ1_YEAST BZZ1_YEAST]] Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.<ref>PMID:12391157</ref> <ref>PMID:16231105</ref>
[https://www.uniprot.org/uniprot/BZZ1_YEAST BZZ1_YEAST] Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.<ref>PMID:12391157</ref> <ref>PMID:16231105</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kursula, I]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Kursula, P]]
[[Category: Kursula I]]
[[Category: Lehmann, F]]
[[Category: Kursula P]]
[[Category: Song, Y H]]
[[Category: Lehmann F]]
[[Category: Wilmanns, M]]
[[Category: Song YH]]
[[Category: Zou, P]]
[[Category: Wilmanns M]]
[[Category: Sh3 domain]]
[[Category: Zou P]]
[[Category: Signaling protein]]

Latest revision as of 16:40, 13 March 2024

Atomic-resolution crystal structure of the second SH3 domain of yeast Bzz1 determined from a pseudomerohedrally twinned crystalAtomic-resolution crystal structure of the second SH3 domain of yeast Bzz1 determined from a pseudomerohedrally twinned crystal

Structural highlights

2a28 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.07Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BZZ1_YEAST Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Soulard A, Lechler T, Spiridonov V, Shevchenko A, Shevchenko A, Li R, Winsor B. Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol Cell Biol. 2002 Nov;22(22):7889-906. PMID:12391157
  2. ↑ Soulard A, Friant S, Fitterer C, Orange C, Kaneva G, Mirey G, Winsor B. The WASP/Las17p-interacting protein Bzz1p functions with Myo5p in an early stage of endocytosis. Protoplasma. 2005 Oct;226(1-2):89-101. Epub 2005 Oct 20. PMID:16231105 doi:http://dx.doi.org/10.1007/s00709-005-0108-4

2a28, resolution 1.07Å

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