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3q28

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{{STRUCTURE_3q28| PDB=3q28 | SCENE= }}
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==Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)==
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===Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)===
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<StructureSection load='3q28' size='340' side='right' caption='[[3q28]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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{{ABSTRACT_PUBMED_21462277}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3q28]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q28 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q25|3q25]], [[3q26|3q26]], [[3q27|3q27]], [[3q29|3q29]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<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=3q28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q28 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q28 RCSB], [http://www.ebi.ac.uk/pdbsum/3q28 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Aggregates of the protein alpha-synuclein are the main component of Lewy bodies, the hallmark of Parkinson's disease. alpha-Synuclein aggregates are also found in many human neurodegenerative diseases known as synucleinopathies. In vivo, alpha-synuclein associates with membranes and adopts alpha-helical conformations. The details of how alpha-synuclein converts from the functional native state to amyloid aggregates remain unknown. In this study, we use maltose-binding protein (MBP) as a carrier to crystallize segments of alpha-synuclein. From crystal structures of fusions between MBP and four segments of alpha-synuclein, we have been able to trace a virtual model of the first 72 residues of alpha-synuclein. Instead of a mostly alpha-helical conformation observed in the lipid environment, our crystal structures show alpha-helices only at residues 1-13 and 20-34. The remaining segments are extended loops or coils. All of the predicted fiber-forming segments based on the 3D profile method are in extended conformations. We further show that the MBP fusion proteins with fiber-forming segments from alpha-synuclein can also form fiber-like nano-crystals or amyloid-like fibrils. Our structures suggest intermediate states during amyloid formation of alpha-synuclein.
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==Function==
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Structures of segments of alpha-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation.,Zhao M, Cascio D, Sawaya MR, Eisenberg D Protein Sci. 2011 Jun;20(6):996-1004. doi: 10.1002/pro.630. Epub 2011 May, 3. PMID:21462277<ref>PMID:21462277</ref>
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[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3q28]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q28 OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021462277</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Cascio, D.]]
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[[Category: Cascio, D]]
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[[Category: Eisenberg, D.]]
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[[Category: Eisenberg, D]]
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[[Category: Sawaya, M R.]]
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[[Category: Sawaya, M R]]
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[[Category: Zhao, M.]]
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[[Category: Zhao, M]]
[[Category: Amyloid]]
[[Category: Amyloid]]
[[Category: Fusion protein]]
[[Category: Fusion protein]]
[[Category: Protein fibril]]
[[Category: Protein fibril]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]

Revision as of 10:16, 19 December 2014

Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)

3q28, resolution 1.60Å

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