1wj9

<table><tr><td colspan='2'>[[1wj9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WJ9 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=1wj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wj9 OCA], [https://pdbe.org/1wj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wj9 RCSB], [https://www.ebi.ac.uk/pdbsum/1wj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wj9 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wj9 TOPSAN]</span></td></tr>

[[https://www.uniprot.org/uniprot/CAS6_THET8 CAS6_THET8]] CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This enzyme processes pre-crRNA into individual crRNA units, but may not actually undergo enzyme turnover, retaining the crRNA product (PubMed:21572442). Generates a 2',3'-cyclic phosphodiester.<ref>PMID:21572442</ref> <ref>PMID:21572444</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

We have determined the crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 at 1.9 A resolution. This protein is a member of the Escherichia coli ygcH sequence family, which contains approximately 15 sequence homologs of bacterial origin. These homologs have a high isoelectric point. The crystal structure reveals that TTHB192 consists of two independently folded domains, and that each domain exhibits a ferredoxin-like fold with a four-stranded antiparallel beta-sheet packed on one side by alpha-helices. These two tandem domains face each other to generate a beta-sheet platform. TTHB192 displays overall structural similarity to Sex-lethal protein and poly(A)-binding protein fragments. These proteins have RNA binding activity which is supported by a beta-sheet platform formed by two tandem repeats of an RNA recognition motif domain with signature sequence motifs on the beta-sheet surface. Although TTHB192 does not have the same signature sequence motif as the RNA recognition motif domain, the presence of an evolutionarily conserved basic patch on the beta-sheet platform could be functionally relevant for nucleic acid-binding. This report shows that TTHB192 and its sequence homologs adopt an RNA recognition motif-like domain and provides the first testable functional hypothesis for this protein family.

Crystal structure of hypothetical protein TTHB192 from Thermus thermophilus HB8 reveals a new protein family with an RNA recognition motif-like domain.,Ebihara A, Yao M, Masui R, Tanaka I, Yokoyama S, Kuramitsu S Protein Sci. 2006 Jun;15(6):1494-9. Epub 2006 May 2. PMID:16672237<ref>PMID:16672237</ref>

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

</div>

<div class="pdbe-citations 1wj9" style="background-color:#fffaf0;"></div>

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Ebihara, A]]

[[Category: Kuramitsu, S]]

[[Category: Structural genomic]]

[[Category: Yao, M]]

[[Category: Yokoyama, S]]

[[Category: Unknown function]]