1mt0

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(New page: 200px<br /><applet load="1mt0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mt0, resolution 2.6&Aring;" /> '''ATP-binding domain of...)
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[[Image:1mt0.jpg|left|200px]]<br /><applet load="1mt0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mt0, resolution 2.6&Aring;" />
 
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'''ATP-binding domain of haemolysin B from Escherichia coli'''<br />
 
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==Overview==
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==ATP-binding domain of hemolysin B from Escherichia coli==
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The ABC-transporter haemolysin B is a central component of the secretion, machinery that translocates the toxin, haemolysin A, in a Sec-independent, fashion across both membranes of E. coli. Here, we report the X-ray, crystal structure of the nucleotide-binding domain (NBD) of HlyB. The, molecule shares the common overall architecture of ABC-transporter NBDs., However, the last three residues of the Walker A motif adopt a 3(10), helical conformation, stabilized by a bound anion. In consequence, this, results in an unusual interaction between the Walker A lysine residue and, the Walker B glutamate residue. As these residues are normally required to, be available for ATP binding, for catalysis and for dimer formation of ABC, domains, we suggest that this conformation may represent a latent, monomeric form of the NBD. Surprisingly, comparison of available NBD, structures revealed a structurally diverse region (SDR) of about 30, residues within the helical arm II domain, unique to each of the eight, NBDs analyzed. As this region interacts with the transmembrane part of, ABC-transporters, the SDR helps to explain the selectivity and/or, targeting of different NBDs to their cognate transmembrane domains.
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<StructureSection load='1mt0' size='340' side='right'caption='[[1mt0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mt0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MT0 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt0 OCA], [https://pdbe.org/1mt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mt0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mt0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HLYBP_ECOLX HLYBP_ECOLX] Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mt/1mt0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mt0 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MT0 OCA].
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*[[Hemolysin 3D structures|Hemolysin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains., Schmitt L, Benabdelhak H, Blight MA, Holland IB, Stubbs MT, J Mol Biol. 2003 Jul 4;330(2):333-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12823972 12823972]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Benabdelhak, H.]]
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[[Category: Benabdelhak H]]
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[[Category: Blight, M.A.]]
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[[Category: Blight MA]]
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[[Category: Holland, I.B.]]
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[[Category: Holland IB]]
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[[Category: Schmitt, L.]]
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[[Category: Schmitt L]]
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[[Category: Stubbs, M.T.]]
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[[Category: Stubbs MT]]
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[[Category: SO4]]
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[[Category: abc-transporter]]
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[[Category: atp-binding domain]]
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[[Category: atp-dependent transport protein]]
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[[Category: haemolysin b]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:40:37 2007''
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Current revision

ATP-binding domain of hemolysin B from Escherichia coli

PDB ID 1mt0

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