2rim is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Histone acetylation plays important roles for the regulation of many fundamental cellular processes. Saccharomyces cerevisiae Rtt109 is an important class of histone acetyltransferases (HATs), which promote genome stability by directly acetylating newly synthesized histone H3 lysine 56 (H3-K56) through an unknown mechanism. Here, we report the crystal structures of Rtt109 at 2.2 A and Rtt109/Acetyl-CoA binary complex at 1.9 A. The structure displays a vise-like topology with mixed three-layered alpha/beta module forming the central module, whose core region resembles the structure of GCN5 HAT domain and P300/CBP HAT domain. Using structural and biochemical analyses, we have discovered the catalytic active site and have identified Asp288 as the deprotonation residue and Lys290 as the autoacetylation residue. We have further proposed the unique H3-K56 anchoring pocket and the potential H3alphaN binding groove. Our work has provided structural insights to understand the acetylation mechanism of H3-K56 by Rtt109.
Structural insights into histone H3 lysine 56 acetylation by Rtt109.,Lin C, Yuan YA Structure. 2008 Oct 8;16(10):1503-10. Epub 2008 Aug 21. PMID:18707894[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Lin C, Yuan YA. Structural insights into histone H3 lysine 56 acetylation by Rtt109. Structure. 2008 Oct 8;16(10):1503-10. Epub 2008 Aug 21. PMID:18707894 doi:10.1016/j.str.2008.07.006
