3puw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3puw.png|left|200px]]


<!--
==Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-AlF4==
The line below this paragraph, containing "STRUCTURE_3puw", creates the "Structure Box" on the page.
<StructureSection load='3puw' size='340' side='right'caption='[[3puw]], [[Resolution|resolution]] 2.30&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'>[[3puw]] is a 5 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=3PUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PUW 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]] 2.3&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</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_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene></td></tr>
{{STRUCTURE_3puw|  PDB=3puw  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3puw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puw OCA], [https://pdbe.org/3puw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puw RCSB], [https://www.ebi.ac.uk/pdbsum/3puw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puw 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(beta,gamma-imido)triphosphate or ADP in conjunction with phosphate analogs , , or , were determined to 2.2- to 2.4-A resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.


===Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-AlF4===
Snapshots of the maltose transporter during ATP hydrolysis.,Oldham ML, Chen J Proc Natl Acad Sci U S A. 2011 Aug 8. PMID:21825153<ref>PMID:21825153</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3puw" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_21825153}}, 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 21825153 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_21825153}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
[[3puw]] is a 5 chain structure with 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=3PUW OCA].
[[Category: Large Structures]]
 
[[Category: Chen J]]
==Reference==
[[Category: Oldham ML]]
<ref group="xtra">PMID:021825153</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Maltose-transporting ATPase]]
[[Category: Chen, J.]]
[[Category: Oldham, M L.]]
[[Category: Abc transporter importer atpase]]
[[Category: Atp binding cassette nucleotide binding domain substrate binding protein transmembrane domain]]
[[Category: Atp binding maltodextrin binding]]
[[Category: Hydrolase-transport protein complex]]
[[Category: Transmembrane integral membrane]]

Latest revision as of 10:05, 13 August 2026

Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-AlF4

3puw, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3puw&oldid=4478270"