1ffh

<table><tr><td colspan='2'>[[1ffh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1FFH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FFH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 ATCC 25104])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ffh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ffh OCA], [http://pdbe.org/1ffh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ffh RCSB], [http://www.ebi.ac.uk/pdbsum/1ffh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ffh ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SRP54_THEAQ SRP54_THEAQ]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY (By similarity).[HAMAP-Rule:MF_00306]

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== Publication Abstract from PubMed ==

The signal-recognition particle (SRP) and its receptor (SR) function in the co-translational targeting of nascent protein-ribosome complexes to the membrane translocation apparatus. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-alpha subunit (termed FtsY). Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other. The sequence of Ffh suggests three domains: an amino-terminal N domain of unknown function, a central GTPase G domain, and a methionine-rich M domain that binds both SRP RNA and signal peptides. Sequence conservation suggests that structurally similar N and G domains are present in FtsY. Here we report the structure of the nucleotide-free form of the NG fragment of Ffh. Consistent with a role for apo Ffh in protein targeting, the side chains of the empty active-site pocket form a tight network of interactions which may stabilize the nucleotide-free protein. The structural relationship between the two domains suggests that the N domain senses or controls the nucleotide occupancy of the GTPase domain. A structural subdomain unique to these evolutionarily conserved GTPases constitutes them as a distinct subfamily in the GTPase superfamily.

Structure of the conserved GTPase domain of the signal recognition particle.,Freymann DM, Keenan RJ, Stroud RM, Walter P Nature. 1997 Jan 23;385(6614):361-4. PMID:9002524<ref>PMID:9002524</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 1ffh" style="background-color:#fffaf0;"></div>

*[[Signal recognition particle protein|Signal recognition particle protein]]

[[Category: Atcc 25104]]

[[Category: Freymann, D M]]

[[Category: Keenan, R J]]

[[Category: Stroud, R M]]

[[Category: Walter, P]]

[[Category: Ffh]]

[[Category: Srp]]