View source for 6lu3


==Crystal structure of a substrate binding protein from Microbacterium hydrocarbonoxydans complexed with 4-hydroxybenzoate hydrazide==
<StructureSection load='6lu3' size='340' side='right'caption='[[6lu3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Microbacterium_hydrocarbonoxydans Microbacterium hydrocarbonoxydans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LU3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HDH:4-OXIDANYLBENZOHYDRAZIDE'>HDH</scene></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=6lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lu3 OCA], [https://pdbe.org/6lu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lu3 RCSB], [https://www.ebi.ac.uk/pdbsum/6lu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lu3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microbacterium hydrocarbonoxydans was isolated, using hydrazide compounds as its sole carbon source. The key enzyme that metabolizes these compounds was identified as hydrazidase, and the operon containing the gene coding for the enzyme, was revealed by genome sequencing. The operon also contained genes coding for an ATP-binding cassette transporter (ABC transporter), which was expected to transport the hydrazide compounds. Substrate binding protein (SBP), a component subunit of the transporter, plays an important role in recognizing the correct substrates for transport. Therefore, to elucidate the mechanism of recognition of the unnatural hydrazide compounds, we determined the crystal structures of the SBP, obtained from M. hydrocarbonoxydans (Mh-SBP), complexed with and without the hydrazide compound, at 2.2 A and 1.75 A resolutions, respectively. The overall structures of Mh-SBP were similar to those of the SBP in oligopeptide transporters such as OppA. On comparison, the liganded and unliganded structures of Mh-SBP showed an open - close conformation change. Interestingly, the binding mode of the compound to Mh-SBP was almost identical to that of the compound to hydrazidase, suggesting that the ABC transporter served transporting these compounds. Furthermore, based on the hydrazide complex structure, paraben, the other putative substrate of the protein, was successfully used with Mh-SBP to obtain the paraben complex structure.

Structural basis of substrate recognition by the substrate binding protein (SBP) of a hydrazide transporter, obtained from Microbacterium hydrocarbonoxydans.,Shimamura K, Akiyama T, Yokoyama K, Takenoya M, Ito S, Sasaki Y, Yajima S Biochem Biophys Res Commun. 2020 Mar 3. pii: S0006-291X(20)30435-6. doi:, 10.1016/j.bbrc.2020.02.146. PMID:32143826<ref>PMID:32143826</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lu3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Microbacterium hydrocarbonoxydans]]
[[Category: Akiyama T]]
[[Category: Ito S]]
[[Category: Sasaki Y]]
[[Category: Shimamura K]]
[[Category: Takenoya M]]
[[Category: Yajima S]]
[[Category: Yokoyama K]]