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5aza

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Revision as of 06:32, 31 May 2023

Crystal structure of MBP-sAglB fusion protein with a 20-residue spacer in the connector helix

Structural highlights

5aza is a 1 chain structure with sequence from Escherichia coli K-12 and Pyrococcus furiosus COM1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.I6V0B8_9EURY

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/5aza"

Categories: Escherichia coli K-12 | Large Structures | Pyrococcus furiosus COM1 | Kohda D | Matsuoka R

@@ Line 3: / Line 3: @@
 <StructureSection load='5aza' size='340' side='right'caption='[[5aza]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5aza]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5aza]] 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/Pyrococcus_furiosus_COM1 Pyrococcus furiosus COM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5az6|5az6]], [[5az7|5az7]], [[5az8|5az8]], [[5az9|5az9]]</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=5aza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aza OCA], [https://pdbe.org/5aza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aza RCSB], [https://www.ebi.ac.uk/pdbsum/5aza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aza ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFC_07420 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5aza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aza OCA], [http://pdbe.org/5aza PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aza RCSB], [http://www.ebi.ac.uk/pdbsum/5aza PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aza 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/I6V0B8_9EURY I6V0B8_9EURY]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Kohda, D]]
+[[Category: Pyrococcus furiosus COM1]]
-[[Category: Matsuoka, R]]
+[[Category: Kohda D]]
-[[Category: Fusion protein]]
+[[Category: Matsuoka R]]
-[[Category: Sugar binding protein]]
-[[Category: Transferase]]

5aza

From Proteopedia

Revision as of 06:32, 31 May 2023

Crystal structure of MBP-sAglB fusion protein with a 20-residue spacer in the connector helix

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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