View source for 5my7


==Adhesin Complex Protein from Neisseria meningitidis==
<StructureSection load='5my7' size='340' side='right'caption='[[5my7]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5my7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MY7 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=5my7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my7 OCA], [https://pdbe.org/5my7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5my7 RCSB], [https://www.ebi.ac.uk/pdbsum/5my7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5my7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9JXD8_NEIMB Q9JXD8_NEIMB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic and commensal Neisseria species produce an Adhesin Complex Protein, which was first characterised in Neisseria meningitidis (Nm) as a novel surface-exposed adhesin with vaccine potential. In the current study, the crystal structure of a recombinant (r)Nm-ACP Type I protein was determined to 1.4 A resolution: the fold resembles an eight-stranded beta-barrel, stabilized by a disulphide bond between the first (Cys38) and last (Cys121) beta-strands. There are few main-chain hydrogen bonds linking beta4-beta5 and beta8-beta1, so the structure divides into two four-stranded anti-parallel beta-sheets (beta1-beta4 and beta5-beta8). The computed surface electrostatic charge distribution showed that the beta1-beta4 sheet face is predominantly basic, whereas the beta5-beta8 sheet is apolar, apart from the loop between beta4 and beta5. Concentrations of rNm-ACP and rNeisseria gonorrhoeae-ACP proteins &gt;/=0.25 mug/ml significantly inhibited by ~80-100% (P&lt;0.05) the in vitro activity of human lysozyme (HL) over 24 h. Specificity was demonstrated by the ability of murine anti-Neisseria ACP sera to block ACP inhibition and restore HL activity. ACP expression conferred tolerance to HL activity, as demonstrated by significant 3-9 fold reductions (P&lt;0.05) in the growth of meningococcal and gonococcal acp gene knock-out mutants in the presence of lysozyme. In addition, wild-type Neisseria lactamica treated with purified ACP-specific rabbit IgG antibodies showed similar fold reductions in bacterial growth, compared with untreated bacteria (P&lt;0.05). Nm-ACPI is structurally similar to the MliC/PliC protein family of lysozyme inhibitors. However, Neisseria ACP proteins show &lt;20% primary sequence similarity with these inhibitors and do not share any conserved MliC/PliC sequence motifs associated with lysozyme recognition. These observations suggest that Neisseria ACP adopts a different mode of lysozyme inhibition and that the ability of ACP to inhibit lysozyme activity could be important for host colonization by both pathogenic and commensal Neisseria organisms. Thus, ACP represents a dual target for developing Neisseria vaccines and drugs to inhibit host-pathogen interactions.

Structure of the Neisseria Adhesin Complex Protein (ACP) and its role as a novel lysozyme inhibitor.,Humbert MV, Awanye AM, Lian LY, Derrick JP, Christodoulides M PLoS Pathog. 2017 Jun 29;13(6):e1006448. doi: 10.1371/journal.ppat.1006448., eCollection 2017 Jun. PMID:28662181<ref>PMID:28662181</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5my7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Awanye A]]
[[Category: Derrick JP]]