1jvx

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[[Image:1jvx.gif|left|200px]]
 
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{{Structure
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==Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal==
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|PDB= 1jvx |SIZE=350|CAPTION= <scene name='initialview01'>1jvx</scene>, resolution 2.50&Aring;
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<StructureSection load='1jvx' size='340' side='right'caption='[[1jvx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>
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<table><tr><td colspan='2'>[[1jvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVX FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE= malE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<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>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvx OCA], [https://pdbe.org/1jvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvx RCSB], [https://www.ebi.ac.uk/pdbsum/1jvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvx ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1mdq|1MDQ]], [[1jvy|1JVY]]
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</table>
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1jvx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jvx RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/1jvx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Maltodextrin-binding protein variant D207C/A301GS/P316C cross-linked in crystal'''
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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<ref>PMID:12538909</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1jvx" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1JVX is a [[Single protein]] structure of 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=1JVX OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12538909 12538909]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bell, J A.]]
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[[Category: Bell JA]]
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[[Category: Iyer, G H.]]
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[[Category: Iyer GH]]
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[[Category: Przybycien, T A.]]
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[[Category: Przybycien TA]]
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[[Category: Samsonoff, W A.]]
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[[Category: Samsonoff WA]]
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[[Category: Srinivasan, U.]]
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[[Category: Srinivasan U]]
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[[Category: cross-link]]
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[[Category: disulfide]]
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[[Category: intermolecular]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:39:46 2008''
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Current revision

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

PDB ID 1jvx

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