This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1jvx

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:15, 11 October 2017

Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal

Structural highlights

1jvx is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1mdq, 1jvy
Gene:	malE ("Bacillus coli" Migula 1895)
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cysteine substitutions were engineered on the surface of maltose binding protein to produce crystine fibers, linear polymers of folded protein formed within a crystal. Disulfide bond formation between adjacent protein molecules within the lattice was monitored by X-ray crystallography. The cross-linked crystals were resistant to dissolution in water or neutral buffer solutions, even though the cross-linking was one-dimensional. However, crystine fibers were observed by transmission electron microscopy to dissociate from the crystals in acidic solutions. Some fibers remained associated as two-dimensional bundles or sheets, with a repeat unit along the fibers consistent with the packing of the individual protein molecules in the crystal. Neutralization of the acidic solutions caused the fibers to re-associate as a solid. Crystine threads were drawn out of this solution. In scanning electron microscopy images, many individual fibers could be seen unwinding from the ends of some threads. Crystine fibers are a new type of biomolecular material with potential applications wherever the use of proteins in a fibrous form is desirable, for example, the incorporation of enzymes into cloth or filtration material.

Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry.,Srinivasan U, Iyer GH, Przybycien TA, Samsonoff WA, Bell JA Protein Eng. 2002 Nov;15(11):895-902. PMID:12538909^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Srinivasan U, Iyer GH, Przybycien TA, Samsonoff WA, Bell JA. Crystine: fibrous biomolecular material from protein crystals cross-linked in a specific geometry. Protein Eng. 2002 Nov;15(11):895-902. PMID:12538909

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jvx"

@@ Line 1: / Line 1: @@
 ==Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal==
 <StructureSection load='1jvx' size='340' side='right' caption='[[1jvx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mdq|1mdq]], [[1jvy|1jvy]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1jvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvx OCA], [http://pdbe.org/1jvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jvx RCSB], [http://www.ebi.ac.uk/pdbsum/1jvx PDBsum]</span></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=1jvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvx OCA], [http://pdbe.org/1jvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jvx RCSB], [http://www.ebi.ac.uk/pdbsum/1jvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvx ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jvx ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1jvx" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Maltose-binding protein|Maltose-binding protein]]
 == References ==
 <references/>

1jvx

From Proteopedia

Revision as of 07:15, 11 October 2017

Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox