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| | <StructureSection load='5az9' size='340' side='right'caption='[[5az9]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='5az9' size='340' side='right'caption='[[5az9]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5az9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZ9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5az9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZ9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5az6|5az6]], [[5az7|5az7]], [[5az8|5az8]], [[5aza|5aza]]</td></tr> | + | </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=5az9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5az9 OCA], [https://pdbe.org/5az9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5az9 RCSB], [https://www.ebi.ac.uk/pdbsum/5az9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5az9 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tomm20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=5az9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5az9 OCA], [http://pdbe.org/5az9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5az9 RCSB], [http://www.ebi.ac.uk/pdbsum/5az9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5az9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [https://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.[https://www.uniprot.org/uniprot/TOM20_RAT TOM20_RAT] Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kohda, D]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Matsuoka, R]] | + | [[Category: Kohda D]] |
| - | [[Category: Fusion protein complex]] | + | [[Category: Matsuoka R]] |
| - | [[Category: Peptide binding protein]]
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| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.TOM20_RAT Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity).
Publication Abstract from PubMed
Contacts with neighboring molecules in protein crystals inevitably restrict the internal motions of intrinsically flexible proteins. The resultant clear electron densities permit model building, as crystallographic snapshot structures. Although these still images are informative, they could provide biased pictures of the protein motions. If the mobile parts are located at a site lacking direct contacts in rationally designed crystals, then the amplitude of the movements can be experimentally analyzed. We propose a fusion protein method, to create crystal contact-free space (CCFS) in protein crystals and to place the mobile parts in the CCFS. Conventional model building fails when large amplitude motions exist. In this study, the mobile parts appear as smeared electron densities in the CCFS, by suitable processing of the X-ray diffraction data. We applied the CCFS method to a highly mobile presequence peptide bound to the mitochondrial import receptor, Tom20, and a catalytically relevant flexible segment in the oligosaccharyltransferase, AglB. These two examples demonstrated the general applicability of the CCFS method to the analysis of the spatial distribution of motions within protein molecules. This article is protected by copyright. All rights reserved.
Rational design of crystal contact-free space in protein crystals for analyzing spatial distribution of motions within protein molecules.,Matsuoka R, Shimada A, Komuro Y, Sugita Y, Kohda D Protein Sci. 2015 Dec 22. doi: 10.1002/pro.2867. PMID:26694222[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsuoka R, Shimada A, Komuro Y, Sugita Y, Kohda D. Rational design of crystal contact-free space in protein crystals for analyzing spatial distribution of motions within protein molecules. Protein Sci. 2015 Dec 22. doi: 10.1002/pro.2867. PMID:26694222 doi:http://dx.doi.org/10.1002/pro.2867
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