3ser: Difference between revisions

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<StructureSection load='3ser' size='340' side='right'caption='[[3ser]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3ser' size='340' side='right'caption='[[3ser]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ser]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SER FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ser]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SER FirstGlance]. <br>
</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.35&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ses|3ses]], [[3set|3set]], [[3seu|3seu]], [[3sev|3sev]], [[3sew|3sew]], [[3sex|3sex]], [[3sey|3sey]]</div></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4034, JW3994, malE ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3ser FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ser OCA], [https://pdbe.org/3ser PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ser RCSB], [https://www.ebi.ac.uk/pdbsum/3ser PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ser ProSAT]</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=3ser FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ser OCA], [https://pdbe.org/3ser PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ser RCSB], [https://www.ebi.ac.uk/pdbsum/3ser PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ser ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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/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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Combining the concepts of synthetic symmetrization with the approach of engineering metal binding sites, we have developed a new crystallization methodology termed metal-mediated synthetic symmetrization. In this method, pairs of histidine or cysteine mutations are introduced on the surface of target proteins, generating crystal lattice contacts or oligomeric assemblies upon coordination with metal. Metal-mediated synthetic symmetrization greatly expands the packing and oligomeric assembly possibilities of target proteins, thereby increasing the chances of growing diffraction-quality crystals. To demonstrate this method, we designed various T4 lysozyme (T4L) and maltose-binding protein (MBP) mutants and co-crystallized them with one of three metal ions: copper (Cu(2+) ), nickel (Ni(2+) ) or zinc (Zn(2+) ). The approach resulted in 16 new crystal structures - 8 for T4L and 8 for MBP - displaying a variety of oligomeric assemblies and packing modes, representing in total 13 new and distinct crystal forms for these proteins. We discuss the potential utility of the method for crystallizing target proteins of unknown structure by engineering in pairs of histidine or cysteine residues. As an alternate strategy, we propose that the varied crystallization-prone forms of T4L or MBP engineered in this work could be used as crystallization chaperones, by fusing them genetically to target proteins of interest.
 
An approach to crystallizing proteins by metal-mediated synthetic symmetrization.,Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO Protein Sci. 2011 Sep 6. doi: 10.1002/pro.727. PMID:21898649<ref>PMID:21898649</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ser" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cascio, D]]
[[Category: Cascio D]]
[[Category: Laganowsky, A]]
[[Category: Laganowsky A]]
[[Category: Sawaya, M R]]
[[Category: Sawaya MR]]
[[Category: Soriaga, A B]]
[[Category: Soriaga AB]]
[[Category: Yeates, T O]]
[[Category: Yeates TO]]
[[Category: Zhao, M]]
[[Category: Zhao M]]
[[Category: Metal-mediated synthetic symmetrization]]
[[Category: Sugar binding protein]]
[[Category: Synthetic symmetrization]]

Latest revision as of 12:49, 1 March 2024

Zn-mediated Polymer of Maltose-binding Protein K26H/K30H by Synthetic SymmetrizationZn-mediated Polymer of Maltose-binding Protein K26H/K30H by Synthetic Symmetrization

Structural highlights

3ser is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
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.

See Also

3ser, resolution 2.35Å

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