1hz4

<table><tr><td colspan='2'>[[1hz4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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>

</td></tr><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>

[[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]

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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:11709169<ref>PMID:11709169</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1hz4" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Clausen, T]]

[[Category: Danot, O]]

[[Category: Huber, R]]

[[Category: Steegborn, C]]

[[Category: Two-helix bundle]]