Structures from the Johnson Lab
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scMtr4
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PDB ID 3L9O
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This is the original 3.4 angstrom apo structure of the RNA helicase Mtr4 from S. cerevisiae as described in Jackson, et. al. (2010). The structure revealed a novel arch-like domain that is required for processing of the 5.8 S rRNA.
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This is an updated refinement of the original Mtr4 structure. Improvements were made primarily in the arch domain after careful alignment to subsequently published higher resolution structures of Mtr4, as described in Taylor, et al (2014).
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S-HPCDH
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These are crystal structures of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH) from Xanthobacter autotrophicus, as described in Bakelar, et al (2013). These structures present a unique case study on how stereospecificity is achieved by two enzymes, allowing them to act exclusively on R- and S- forms of the same substrate.
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PTP1B
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These crystal structures represent various transition states for human Protein Tyrosine Phosphatase 1B (PTP1B). The enzyme goes through a 2-step mechanism involving a phosphocysteine intermediate. These structures, combined with previously determined structures allowed us to outline "snapshots" of a complete catalytic cycle. This is a collaborative work with the Hengge lab described in Brandao, et al (2010).
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These structures of a WPD-loop mutant, described in Brandao, et al (2012), were used to describe the molecular details of loop movement in PTP1B. Significantly, this work demonstrated that while PTP1B and YopH (described below) both utilize a WPD-loop, the details of loop movement differ between the two enyzmes.
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YopH
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This series of structures of crystal structures from Yersinia protein-tyrosine phosphatase YopH show how a simple tyrosine to phenylalanine mutation can reduce the catalytic rate of this extremely fast enzyme by more than two orders of magnitude. This is a collaborative work with the Hengge lab described in Brandao, et al (2009).
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PRMT1
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PDB ID 3Q7E
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This crystal structure of rat Protein Arginine Methyltransferase 1 (PRMT1) reveals the structural effect of mutating a conserved active site methionine. This collaborative work with the Hevel lab, described in Gui, et al (2011), provides important insight into how product specificity is achieved.
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VHZ
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PDB ID 4ERC
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This 1.1 angstrom crystal structure of the human VHZ protein led to the reclassification of this small enzyme as an atypical protein tyrosine phosphatase. This collaborative work with the Hengge lab was published in Kuznetsov, et al, (2012).
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