3mbp: Difference between revisions

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-{{Seed}}
-[[Image:3mbp.png|left|200px]]
-<!--
+==MALTODEXTRIN-BINDING PROTEIN WITH BOUND MALTOTRIOSE==
-The line below this paragraph, containing "STRUCTURE_3mbp", creates the "Structure Box" on the page.
+<StructureSection load='3mbp' size='340' side='right'caption='[[3mbp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3mbp]] is a 1 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=3MBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MBP FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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_900009:alpha-maltotriose'>PRD_900009</scene></td></tr>
-{{STRUCTURE_3mbp|  PDB=3mbp  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3mbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mbp OCA], [https://pdbe.org/3mbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mbp RCSB], [https://www.ebi.ac.uk/pdbsum/3mbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mbp ProSAT]</span></td></tr>
+</table>
+== 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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/3mbp_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <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/main_output.php?pdb_ID=3mbp ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: Active-transport processes perform a vital function in the life of a cell, maintaining cell homeostasis and allowing access of nutrients. Maltodextrin/maltose-binding protein (MBP; M(r) = 40k) is a receptor protein which serves as an initial high-affinity binding component of the active-transport system of maltooligosaccharides in bacteria. MBP also participates in chemotaxis towards maltooligosaccharides. The interaction between MBP and specific cytoplasmic membrane proteins initiates either active transport or chemotaxis. In order to gain new understanding of the function of MBP, especially its versatility in binding different linear and cyclic oligosaccharides with similar affinities, we have undertaken high-resolution X-ray analysis of three oligosaccharide-bound structures. RESULTS: The structures of MBP complexed with maltose, maltotriose and maltotetraose have been refined to high resolutions (1.67 to 1.8 A). These structures provide details at the atomic level of many features of oligosaccharide binding. The structures reveal differences between buried and surface binding sites and show the importance of hydrogen bonds and van der Waals interactions, especially those resulting from aromatic residue stacking. Insights are provided into the structural plasticity of the protein, the binding affinity and the binding specificity with respect to alpha/beta anomeric preference and oligosaccharide length. In addition, the structures demonstrate the different conformations that can be adopted by the oligosaccharide within the complex. CONCLUSIONS: MBP has a two-domain structure joined by a hinge-bending region which contains the substrate-binding groove. The bound maltooligosaccharides have a ribbon-like structure: the edges of the ribbon are occupied by polar hydroxyl groups and the flat surfaces are composed of nonpolar patches of the sugar ring faces. The polar groups and nonpolar patches are heavily involved in forming hydrogen bonds and van der Waals contacts, respectively, with complimentary residues in the groove. Hinge-bending between the two domains enables the participation of both domains in the binding and sequestering of the oligosaccharides. Changes in the subtle contours of the binding site allow binding of maltodextrins of varying length with similarly high affinities. The fact that the three bound structures are essentially identical ensures productive interaction with the oligomeric membrane proteins, which are distinct for transport and chemotaxis.
-===MALTODEXTRIN-BINDING PROTEIN WITH BOUND MALTOTRIOSE===
+Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.,Quiocho FA, Spurlino JC, Rodseth LE Structure. 1997 Aug 15;5(8):997-1015. PMID:9309217<ref>PMID:9309217</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3mbp" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9309217}}, adds the Publication Abstract to the page
+*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9309217 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9309217}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli K-12]]
-MBP is a 1 chain 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=3MBP OCA].
+[[Category: Large Structures]]
+[[Category: Quiocho FA]]
-==Reference==
+[[Category: Spurlino JC]]
-<ref group="xtra">PMID:9309217</ref><references group="xtra"/>
-[[Category: Escherichia coli]]
-[[Category: Quiocho, F A.]]
-[[Category: Spurlino, J C.]]
-[[Category: Periplasmic binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 19:58:33 2009''