View source for 1mmc


==1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2==
<StructureSection load='1mmc' size='340' side='right'caption='[[1mmc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Amaranthus_caudatus Amaranthus caudatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 26 models</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=1mmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmc OCA], [https://pdbe.org/1mmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmc RCSB], [https://www.ebi.ac.uk/pdbsum/1mmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMP_AMACA AMP_AMACA] Chitin-binding protein with a defensive function against numerous chitin containing fungal pathogens. It is also a potent inhibitor of Gram-positive bacteria.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein.

H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.,Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P J Mol Biol. 1996 May 3;258(2):322-33. PMID:8627629<ref>PMID:8627629</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mmc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Amaranthus caudatus]]
[[Category: Large Structures]]
[[Category: Loris R]]
[[Category: Maes D]]
[[Category: Martins JC]]
[[Category: Pepermans HAM]]
[[Category: Verheyden P]]
[[Category: Willem R]]
[[Category: Wyns L]]