View source for 6xj7


==Crystal structure of the helical cell shape determining protein Pgp2 (K307A mutant) from Campylobacter jejuni==
<StructureSection load='6xj7' size='340' side='right'caption='[[6xj7]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_81-176 Campylobacter jejuni subsp. jejuni 81-176]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XJ7 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]] 1.85&#8491;</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=6xj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xj7 OCA], [https://pdbe.org/6xj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xj7 RCSB], [https://www.ebi.ac.uk/pdbsum/6xj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xj7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H3PAQ3_CAMJJ A0A0H3PAQ3_CAMJJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The helical morphology of Campylobacter jejuni, a bacterium involved in host gut colonization and pathogenesis in humans, is determined by the structure of the peptidoglycan (PG) layer. This structure is dictated by trimming of peptide stems by the LD-carboxypeptidase Pgp2 within the periplasm. The interaction interface between Pgp2 and PG to select sites for peptide trimming is unknown. We determined a 1.6 A resolution crystal structure of Pgp2, which contains a conserved LD-carboxypeptidase domain and a previously uncharacterized domain with an NTF2-like fold (NTF2). We identified a pocket in the NTF2 domain formed by conserved residues and located approximately 40 A from the LD-carboxypeptidase active site. Expression of pgp2 in trans with substitutions of charged (Lys257, Lys307, Glu324) and hydrophobic residues (Phe242 and Tyr233) within the pocket did not restore helical morphology to a pgp2 deletion strain. Muropeptide analysis indicated a decrease of murotripeptides in the deletion strain expressing these mutants, suggesting reduced Pgp2 catalytic activity. Pgp2 but not the K307A mutant was pulled down by C. jejuni Deltapgp2 PG sacculi, supporting a role for the pocket in PG binding. NMR spectroscopy was used to define the interaction interfaces of Pgp2 with several PG fragments, which bound to the active site within the LD-carboxypeptidase domain and the pocket of the NTF2 domain. We propose a model for Pgp2 binding to PG strands involving both the LD-carboxypeptidase domain and the accessory NTF2 domain to induce a helical cell shape.

Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni.,Sheng-Huei Lin C, Chan ACK, Vermeulen J, Brockerman J, Soni AS, Tanner ME, Gaynor EC, McIntosh LP, Simorre JP, Murphy MEP J Biol Chem. 2021 Mar 9:100528. doi: 10.1016/j.jbc.2021.100528. PMID:33711341<ref>PMID:33711341</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xj7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Campylobacter jejuni subsp. jejuni 81-176]]
[[Category: Large Structures]]
[[Category: Chan AC]]
[[Category: Lin CS]]
[[Category: Murphy ME]]