View source for 5icq


==Methanobactin periplasmic binding protein==
<StructureSection load='5icq' size='340' side='right'caption='[[5icq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5icq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_parvus_OBBP Methylocystis parvus OBBP]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ICQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ICQ 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]] 1.9&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5icq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5icq OCA], [https://pdbe.org/5icq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5icq RCSB], [https://www.ebi.ac.uk/pdbsum/5icq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5icq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1L1QK06_9HYPH A0A1L1QK06_9HYPH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Methanotrophic bacteria use methane, a potent greenhouse gas, as their primary source of carbon and energy. The first step in methane metabolism is its oxidation to methanol. In almost all methanotrophs, this chemically challenging reaction is catalyzed by particulate methane monooxygenase (pMMO), a copper-dependent integral membrane enzyme. Methanotrophs acquire copper (Cu) for pMMO by secreting a small ribosomally produced, posttranslationally modified natural product called methanobactin (Mbn). Mbn chelates Cu with high affinity, and the Cu-loaded form (CuMbn) is reinternalized into the cell via an active transport process. Bioinformatic and gene regulation studies suggest that two proteins might play a role in CuMbn handling: the TonB-dependent transporter MbnT and the periplasmic binding protein MbnE. Disruption of the gene that encodes MbnT abolishes CuMbn uptake, as reported previously, and expression of MbnT in Escherichia coli confers the ability to take up CuMbn. Biophysical studies of MbnT and MbnE reveal specific interactions with CuMbn, and a crystal structure of apo MbnE is consistent with MbnE's proposed role as a periplasmic CuMbn transporter. Notably, MbnT and MbnE exhibit different levels of discrimination between cognate and noncognate CuMbns. These findings provide evidence for CuMbn-protein interactions and begin to elucidate the molecular mechanisms of its recognition and transport.

Methanobactin transport machinery.,Dassama LM, Kenney GE, Ro SY, Zielazinski EL, Rosenzweig AC Proc Natl Acad Sci U S A. 2016 Nov 15;113(46):13027-13032. Epub 2016 Nov 2. PMID:27807137<ref>PMID:27807137</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5icq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylocystis parvus OBBP]]
[[Category: Dassama LMK]]
[[Category: Rosenzweig AC]]