1q1b: Difference between revisions

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-[[Image:1q1b.jpg|left|200px]]
-<!--
+==Crystal structure of E. coli MalK in the nucleotide-free form==
-The line below this paragraph, containing "STRUCTURE_1q1b", creates the "Structure Box" on the page.
+<StructureSection load='1q1b' size='340' side='right'caption='[[1q1b]], [[Resolution|resolution]] 2.80&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'>[[1q1b]] is a 4 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=1Q1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1B 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]] 2.8&#8491;</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=1q1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1b OCA], [https://pdbe.org/1q1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1b RCSB], [https://www.ebi.ac.uk/pdbsum/1q1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1b ProSAT]</span></td></tr>
-{{STRUCTURE_1q1b|  PDB=1q1b  |  SCENE=  }}
+</table>
+== Function ==
-'''Crystal structure of E. coli MalK in the nucleotide-free form'''
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
-==Overview==
+Check<jmol>
-The ATPase components of ATP binding cassette (ABC) transporters power the transporters by binding and hydrolyzing ATP. Major conformational changes of an ATPase are revealed by crystal structures of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, in three different dimeric configurations. While other nucleotide binding domains or subunits display low affinity for each other in the absence of the transmembrane segments, the MalK dimer is stabilized through interactions of the additional C-terminal domains. In the two nucleotide-free structures, the N-terminal nucleotide binding domains are separated to differing degrees, and the dimer is maintained through contacts of the C-terminal regulatory domains. In the ATP-bound form, the nucleotide binding domains make contact and two ATPs lie buried along the dimer interface. The two nucleotide binding domains of the dimer open and close like a pair of tweezers, suggesting a regulatory mechanism for ATPase activity that may be tightly coupled to translocation.
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/1q1b_consurf.spt"</scriptWhenChecked>
-==About this Structure==
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-Q1B 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=1Q1B OCA].
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
-==Reference==
+</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=1q1b ConSurf].
-A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle., Chen J, Lu G, Lin J, Davidson AL, Quiocho FA, Mol Cell. 2003 Sep;12(3):651-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14527411 14527411]
+<div style="clear:both"></div>
-[[Category: Escherichia coli]]
+__TOC__
-[[Category: Single protein]]
+</StructureSection>
-[[Category: Chen, J.]]
+[[Category: Escherichia coli K-12]]
-[[Category: Davidson, A L.]]
+[[Category: Large Structures]]
-[[Category: Lin, J.]]
+[[Category: Chen J]]
-[[Category: Lu, G.]]
+[[Category: Davidson AL]]
-[[Category: Quiocho, F A.]]
+[[Category: Lin J]]
-[[Category: Nucleotide-free form]]
+[[Category: Lu G]]
-[[Category: Semi-open dimer]]
+[[Category: Quiocho FA]]
-[[Category: Sugar transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:44:38 2008''