4ki0: Difference between revisions

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-{{STRUCTURE_4ki0|  PDB=4ki0  |  SCENE=  }}
-===Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to maltohexaose===
-{{ABSTRACT_PUBMED_24145421}}
-==Function==
+==Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to maltohexaose==
-[[http://www.uniprot.org/uniprot/MALF_ECOLI MALF_ECOLI]] Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. [[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.
+<StructureSection load='4ki0' size='340' side='right'caption='[[4ki0]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ki0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1] and [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=4KI0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KI0 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGV:(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+(11E)-OCTADEC-11-ENOATE'>PGV</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene></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=4ki0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ki0 OCA], [https://pdbe.org/4ki0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ki0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ki0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ki0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MALK_ECOLI MALK_ECOLI] Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+ATP-binding cassette (ABC) transporters are molecular pumps that harness the chemical energy of ATP hydrolysis to translocate solutes across the membrane. The substrates transported by different ABC transporters are diverse, ranging from small ions to large proteins. Although crystal structures of several ABC transporters are available, a structural basis for substrate recognition is still lacking. For the Escherichia coli maltose transport system, the selectivity of sugar binding to maltose-binding protein (MBP), the periplasmic binding protein, does not fully account for the selectivity of sugar transport. To obtain a molecular understanding of this observation, we determined the crystal structures of the transporter complex MBP-MalFGK2 bound with large malto-oligosaccharide in two different conformational states. In the pretranslocation structure, we found that the transmembrane subunit MalG forms two hydrogen bonds with malto-oligosaccharide at the reducing end. In the outward-facing conformation, the transmembrane subunit MalF binds three glucosyl units from the nonreducing end of the sugar. These structural features explain why modified malto-oligosaccharides are not transported by MalFGK2 despite their high binding affinity to MBP. They also show that in the transport cycle, substrate is channeled from MBP into the transmembrane pathway with a polarity such that both MBP and MalFGK2 contribute to the overall substrate selectivity of the system.
-==About this Structure==
+Structural basis for substrate specificity in the Escherichia coli maltose transport system.,Oldham ML, Chen S, Chen J Proc Natl Acad Sci U S A. 2013 Oct 21. PMID:24145421<ref>PMID:24145421</ref>
-[[4ki0]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecod1 Ecod1] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KI0 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<ref group="xtra">PMID:024145421</ref><references group="xtra"/><references/>
+</div>
-[[Category: Ecod1]]
+<div class="pdbe-citations 4ki0" style="background-color:#fffaf0;"></div>
-[[Category: Ecoli]]
-[[Category: Chen, J.]]
+==See Also==
-[[Category: Chen, S.]]
+*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]]
-[[Category: Oldham, M L.]]
+== References ==
-[[Category: Abc transporter]]
+<references/>
-[[Category: Atp binding maltodextrin binding]]
+__TOC__
-[[Category: Atpase maltodextrin transporter]]
+</StructureSection>
-[[Category: Inner membrane]]
+[[Category: Escherichia coli DH1]]
-[[Category: Transport protein]]
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Chen J]]
+[[Category: Chen S]]
+[[Category: Oldham ML]]