5az6

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of MBP-Tom20 fusion protein with a 2-residue spacer in the connector helix

Structural highlights

5az6 is a 2 chain structure with sequence from Escherichia coli K-12 and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.56Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5az6"

Categories: Escherichia coli K-12 | Large Structures | Rattus norvegicus | Kohda D | Matsuoka R

@@ Line 1: / Line 1: @@
 ==Crystal structure of MBP-Tom20 fusion protein with a 2-residue spacer in the connector helix==
-<StructureSection load='5az6' size='340' side='right' caption='[[5az6]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
+<StructureSection load='5az6' size='340' side='right'caption='[[5az6]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5az6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZ6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5az6]] is a 2 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=5AZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZ6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></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]] 2.56&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5az7|5az7]], [[5az8|5az8]], [[5az9|5az9]], [[5aza|5aza]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></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=5az6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5az6 OCA], [http://pdbe.org/5az6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5az6 RCSB], [http://www.ebi.ac.uk/pdbsum/5az6 PDBsum]</span></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=5az6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5az6 OCA], [https://pdbe.org/5az6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5az6 RCSB], [https://www.ebi.ac.uk/pdbsum/5az6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5az6 ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Kohda, D]]
+[[Category: Escherichia coli K-12]]
-[[Category: Matsuoka, R]]
+[[Category: Large Structures]]
-[[Category: Fusion protein]]
+[[Category: Rattus norvegicus]]
-[[Category: Peptide binding protein]]
+[[Category: Kohda D]]
-[[Category: Sugar binding protein]]
+[[Category: Matsuoka R]]

5az6

From Proteopedia

Current revision

Crystal structure of MBP-Tom20 fusion protein with a 2-residue spacer in the connector helix

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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