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==Crystal Structure of the MABP Domain of MVB12B of Human ESCRT-I Complex== | |||
<StructureSection load='3tow' size='340' side='right' caption='[[3tow]], [[Resolution|resolution]] 1.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tow]] is a 1 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=3TOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TOW FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C9orf28, FAM125B, MVB12B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3tow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tow OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tow RCSB], [http://www.ebi.ac.uk/pdbsum/3tow PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MVB12-associated beta-prism (MABP) domains are predicted to occur in a diverse set of membrane-associated bacterial and eukaryotic proteins, but their existence, structure, and biochemical properties have not been characterized experimentally. Here, we find that the MABP domains of the MVB12A and B subunits of ESCRT-I are functional modules that bind in vitro to liposomes containing acidic lipids depending on negative charge density. The MABP domain is capable of autonomously localizing to subcellular puncta and to the plasma membrane. The 1.3-A atomic resolution crystal structure of the MVB12B MABP domain reveals a beta-prism fold, a hydrophobic membrane-anchoring loop, and an electropositive phosphoinositide-binding patch. The basic patch is open, which explains how it senses negative charge density but lacks stereoselectivity. These observations show how ESCRT-I could act as a coincidence detector for acidic phospholipids and protein ligands, enabling it to function both in protein transport at endosomes and in cytokinesis and viral budding at the plasma membrane. | |||
Structural basis for membrane targeting by the MVB12-associated beta-prism domain of the human ESCRT-I MVB12 subunit.,Boura E, Hurley JH Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):1901-6. Epub 2012 Jan 9. PMID:22232651<ref>PMID:22232651</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Boura, E | [[Category: Boura, E]] | ||
[[Category: Hurley, J H | [[Category: Hurley, J H]] | ||
[[Category: Beta prism]] | [[Category: Beta prism]] | ||
[[Category: Membrane binding domain]] | [[Category: Membrane binding domain]] | ||
[[Category: Negatively charged membrane]] | [[Category: Negatively charged membrane]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
Revision as of 21:17, 21 December 2014
Crystal Structure of the MABP Domain of MVB12B of Human ESCRT-I ComplexCrystal Structure of the MABP Domain of MVB12B of Human ESCRT-I Complex
Structural highlights
Publication Abstract from PubMedMVB12-associated beta-prism (MABP) domains are predicted to occur in a diverse set of membrane-associated bacterial and eukaryotic proteins, but their existence, structure, and biochemical properties have not been characterized experimentally. Here, we find that the MABP domains of the MVB12A and B subunits of ESCRT-I are functional modules that bind in vitro to liposomes containing acidic lipids depending on negative charge density. The MABP domain is capable of autonomously localizing to subcellular puncta and to the plasma membrane. The 1.3-A atomic resolution crystal structure of the MVB12B MABP domain reveals a beta-prism fold, a hydrophobic membrane-anchoring loop, and an electropositive phosphoinositide-binding patch. The basic patch is open, which explains how it senses negative charge density but lacks stereoselectivity. These observations show how ESCRT-I could act as a coincidence detector for acidic phospholipids and protein ligands, enabling it to function both in protein transport at endosomes and in cytokinesis and viral budding at the plasma membrane. Structural basis for membrane targeting by the MVB12-associated beta-prism domain of the human ESCRT-I MVB12 subunit.,Boura E, Hurley JH Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):1901-6. Epub 2012 Jan 9. PMID:22232651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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