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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.83 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-08 Revision Date: Molecular Weight:43628.65 Macromolecule Type:Protein Residue Count:372 Atom Site Count:2976 DOI:10.2210/pdb5n32/pdb
Data Types:
  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.25 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-02-11 Revision Date: Molecular Weight:37433.66 Macromolecule Type:Protein Residue Count:327 Atom Site Count:2187 DOI:10.2210/pdb5n52/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.4 Classification:TRANSCRIPTION Release Date:2018-02-28 Deposition Date:2018-01-26 Revision Date: Molecular Weight:171377.12 Macromolecule Type:Protein Residue Count:1465 Atom Site Count:7947 DOI:10.2210/pdb5z72/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.0 Classification:TRANSFERASE Release Date:2018-02-28 Deposition Date:2017-08-22 Revision Date: Molecular Weight:44726.75 Macromolecule Type:Protein Residue Count:387 Atom Site Count:3135 DOI:10.2210/pdb5y92/pdb Abstract: Catharanthus roseus Receptor-Like Kinase 1-like (CrRLK1L) proteins contain two tandem malectin-like modules in their extracellular domains (ECDs) and function in diverse signaling pathways in plants. Malectin is a carbohydrate-binding protein in animals and recognizes a number of diglucosides; however, it remains unclear how the two malectin-like domains in the CrRLK1L proteins sense the ligand molecule. In this study, we reveal the crystal structures of the ECDs of ANXUR1 and ANXUR2, two CrRLK1L members in Arabidopsis thaliana that have critical functions in controlling pollen tube rupture during the fertilization process. We show that the two malectin-like domains in these proteins pack together to form a rigid architecture. Unlike animal malectin, these malectin-like domains lack residues involved in binding to the diglucosides, suggesting that they have a distinct ligand-binding mechanism. A cleft is observed between the two malectin-like domains, which might function as a potential ligand-binding pocket. This article is protected by copyright. All rights reserved.
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:3.8 Classification:VIRAL PROTEIN Release Date:2018-02-28 Deposition Date:2017-09-03 Revision Date: Molecular Weight:71180.09 Macromolecule Type:Protein Residue Count:584 Atom Site Count:3495 DOI:10.2210/pdb5yb2/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.19 Classification:TRANSFERASE/ANTIBIOTIC Release Date:2018-02-28 Deposition Date:2017-10-20 Revision Date: Molecular Weight:32858.33 Macromolecule Type:Protein Residue Count:302 Atom Site Count:2063 DOI:10.2210/pdb6bc2/pdb
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.85 Classification:OXIDOREDUCTASE Release Date:2018-02-28 Deposition Date:2017-06-29 Revision Date: Molecular Weight:104168.63 Macromolecule Type:Protein Residue Count:922 Atom Site Count:7006 DOI:10.2210/pdb5oc2/pdb Abstract: Amadoriases are a class of FAD-dependent enzymes that are found in fungi, yeast and bacteria and that are able to hydrolyze glycated amino acids, cleaving the sugar moiety from the amino acidic portion. So far, engineered Amadoriases have mostly found practical application in the measurement of the concentration of glycated albumin in blood samples. However, these engineered forms of Amadoriases show relatively low absolute activity and stability levels, which affect their conditions of use. Therefore, enzyme stabilization is desirable prior to function-altering molecular engineering. In this work, we describe a rational design strategy based on a computational screening method to evaluate a library of potentially stabilizing disulfide bonds. Our approach allowed the identification of two thermostable Amadoriase I mutants (SS03 and SS17) featuring a significantly higher T
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Experimental Technique/Method:X-RAY DIFFRACTION Resolution:3.4 Classification:TRANSCRIPTION Release Date:2018-02-28 Deposition Date:2017-11-13 Revision Date: Molecular Weight:481872.03 Macromolecule Type:Protein#DNA#RNA Residue Count:4211 Atom Site Count:28244 DOI:10.2210/pdb6bm2/pdb
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  • Tabular Data
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.29 Classification:HYDROLASE, LYASE/DNA Release Date:2018-02-28 Deposition Date:2017-07-31 Revision Date: Molecular Weight:75354.59 Macromolecule Type:Protein#DNA Residue Count:593 Atom Site Count:5276 DOI:10.2210/pdb5wn2/pdb Abstract: Human apurinic/apyrimidinic (AP) endonuclease 1 (APE1) is an essential DNA repair enzyme which uses a single active site to process DNA damage via two distinct activities: (1) AP-endonuclease and (2) 3' to 5' exonuclease. The AP-endonuclease activity cleaves at AP-sites, while the exonuclease activity excises bulkier 3' mismatches and DNA damage to generate clean DNA ends suitable for downstream repair. Molecular details of the exonuclease reaction and how one active site can accommodate various toxic DNA repair intermediates remains elusive despite being biologically important. Here, we report multiple high-resolution APE1-DNA structural snapshots revealing how APE1 removes 3' mismatches and DNA damage by placing the 3' group within the intra-helical DNA cavity via a non-base flipping mechanism. This process is facilitated by a DNA nick, instability of a mismatched/damaged base, and bending of the DNA. These results illustrate how APE1 cleanses DNA dirty-ends to generate suitable substrates for downstream repair enzymes.
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Experimental Technique/Method:ELECTRON MICROSCOPY Resolution:4.4 Classification:MEMBRANE PROTEIN Release Date:2018-02-28 Deposition Date:2018-02-05 Revision Date: Molecular Weight:506808.34 Macromolecule Type:Protein Residue Count:4550 Atom Site Count:30549 DOI:10.2210/pdb6fo2/pdb
Data Types:
  • Tabular Data
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