1hz4

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(New page: 200px<br /><applet load="1hz4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hz4, resolution 1.45&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hz4.jpg|left|200px]]<br /><applet load="1hz4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hz4, resolution 1.45&Aring;" />
 
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'''CRYSTAL STRUCTURE OF TRANSCRIPTION FACTOR MALT DOMAIN III'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF TRANSCRIPTION FACTOR MALT DOMAIN III==
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BACKGROUND: MalT from Escherichia coli, the best-studied member of the, MalT family of ATP-dependent transcriptional activators, regulates the, genes for malto-oligosaccharide utilization. The active form of this 4, domain protein is a homooligomer, and its multimerization is induced by, the binding of maltotriose. Domains II and III of MalT were suggested to, mediate the oligomerization process, but its molecular mechanism and the, specific functions of these domains remain to be identified. RESULTS: We, solved the crystal structure of MalT domain III at 1.45 A resolution by, multiple isomorphous replacement phasing. The structure reveals eight, copies of a two-helix bundle motif arranged in a novel, right-handed, superhelix fold with closed walls, followed by a small C-terminal, subdomain. The MalT superhelix contains a potential maltotriose binding, site and forms a large hydrophobic protein-protein interaction interface, that mediates the contact between two MalT domain III molecules., Structure-based analysis of the two-helix bundle motifs revealed a novel, degenerated sequence pattern, and repeats of this pattern could be, identified in other regulator proteins. CONCLUSIONS: MalT domain III, contains a novel superhelix fold. Its protein-protein interaction, interface, however, resembles protein binding sites of other superhelical, proteins, suggesting a model with domain III mediating MalT, oligomerization. Maltotriose seems to modulate the interaction interface, and MalT oligomerization by occupying the ligand binding site inside the, superhelix. Similar structural and mechanistic features in other MalT, protein-family members and unrelated regulator proteins are indicated by, the reappearance of a novel sequence motif derived from the MalT domain, III structure.
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<StructureSection load='1hz4' size='340' side='right'caption='[[1hz4]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hz4]] 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=1HZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HZ4 FirstGlance]. <br>
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1HZ4 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, BEZ and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HZ4 OCA].
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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]] 1.45&#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=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1hz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hz4 OCA], [https://pdbe.org/1hz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hz4 RCSB], [https://www.ebi.ac.uk/pdbsum/1hz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hz4 ProSAT]</span></td></tr>
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Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization., Steegborn C, Danot O, Huber R, Clausen T, Structure. 2001 Nov;9(11):1051-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11709169 11709169]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MALT_ECOLI MALT_ECOLI] Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides. Binds and recognizes a DNA motif (called the malT box): 5'-GGA[TG]GA-3'.[HAMAP-Rule:MF_01247]
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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/hz/1hz4_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=1hz4 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[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: Clausen, T.]]
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[[Category: Clausen T]]
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[[Category: Danot, O.]]
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[[Category: Danot O]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Steegborn, C.]]
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[[Category: Steegborn C]]
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[[Category: BEZ]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: helix repeats]]
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[[Category: protein superhelix]]
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[[Category: two-helix bundles]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:55:24 2007''
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Current revision

CRYSTAL STRUCTURE OF TRANSCRIPTION FACTOR MALT DOMAIN III

PDB ID 1hz4

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