1apa

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

</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=1apa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apa OCA], [https://pdbe.org/1apa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apa RCSB], [https://www.ebi.ac.uk/pdbsum/1apa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apa ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RIPA_PHYAM RIPA_PHYAM]] Inhibits viral infection of plants, and protein synthesis in vitro. Has also been shown to inhibit the replication of mammalian viruses. The protein may provide a means of cellular suicide upon invasion by a virus.

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== Publication Abstract from PubMed ==

We have determined the crystal structure of alpha-pokeweed antiviral protein, a member of ribosome-inactivating proteins, at 0.23 nm resolution, by the molecular-replacement method. The crystals belong to the space group P2(1)2(1)2 with unit-cell dimensions a = 4.71, b = 11.63 and c = 4.96 nm, and contain one protein molecule/asymmetric unit based on a crystal volume/unit protein molecular mass of 2.1 x 10(-3) nm3/Da. The crystallographic residual value was reduced to 17.2% (0.6-0.23 nm resolution) with root-mean-square deviations in bond lengths of 1.9 pm and bond angles of 2.2 degrees. The C alpha-C alpha distance map shows that alpha-pokeweed antiviral protein is composed of three modules, the N-terminal (Ala1-Leu76), the central (Tyr77-Lys185) and the C-terminal (Tyr186-Thr266) modules. The substrate-binding site is formed as a cleft between the central and C-terminal modules and all the active residues exist on the central module. The electrostatic potential around the substrate-binding site shows that the central and C-terminal module sides of this cleft have a negatively and a positively charged region, respectively. This charge distribution in the protein seems to provide a suitable interaction with the substrate rRNA.

X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23 nm resolution. A model structure provides a suitable electrostatic field for substrate binding.,Ago H, Kataoka J, Tsuge H, Habuka N, Inagaki E, Noma M, Miyano M Eur J Biochem. 1994 Oct 1;225(1):369-74. PMID:7925458<ref>PMID:7925458</ref>

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

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<div class="pdbe-citations 1apa" style="background-color:#fffaf0;"></div>

*[[Ribosome inactivating protein|Ribosome inactivating protein]]

[[Category: American pokeweed]]

[[Category: Ago, H]]

[[Category: Habuka, N]]

[[Category: Inagaki, E]]

[[Category: Kataoka, J]]

[[Category: Miyano, M]]

[[Category: Noma, M]]

[[Category: Tsuge, H]]

[[Category: Genomic clone]]