6zqp

<table><tr><td colspan='2'>[[6zqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZQP FirstGlance]. <br>

== Function ==

[https://www.uniprot.org/uniprot/PMT2_YEAST PMT2_YEAST] Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.<ref>PMID:15377669</ref> <ref>PMID:18182384</ref> <ref>PMID:21147851</ref> <ref>PMID:8543034</ref>

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

== Publication Abstract from PubMed ==

Protein O-mannosyltransferases (PMTs) represent a conserved family of multispanning endoplasmic reticulum membrane proteins involved in glycosylation of S/T-rich protein substrates and unfolded proteins. PMTs work as dimers and contain a luminal MIR domain with a beta-trefoil fold, which is susceptive for missense mutations causing alpha-dystroglycanopathies in humans. Here, we analyze PMT-MIR domains by an integrated structural biology approach using X-ray crystallography and NMR spectroscopy and evaluate their role in PMT function in vivo. We determine Pmt2- and Pmt3-MIR domain structures and identify two conserved mannose-binding sites, which are consistent with general beta-trefoil carbohydrate-binding sites (alpha, beta), and also a unique PMT2-subfamily exposed FKR motif. We show that conserved residues in site alpha influence enzyme processivity of the Pmt1-Pmt2 heterodimer in vivo. Integration of the data into the context of a Pmt1-Pmt2 structure and comparison with homologous beta-trefoil - carbohydrate complexes allows for a functional description of MIR domains in protein O-mannosylation.

Functional implications of MIR domains in protein O-mannosylation.,Chiapparino A, Grbavac A, Jonker HR, Hackmann Y, Mortensen S, Zatorska E, Schott A, Stier G, Saxena K, Wild K, Schwalbe H, Strahl S, Sinning I Elife. 2020 Dec 24;9. pii: 61189. doi: 10.7554/eLife.61189. PMID:33357379<ref>PMID:33357379</ref>

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

</div>

<div class="pdbe-citations 6zqp" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Saccharomyces cerevisiae]]