2024 |
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Molecular basis of hemoglobin capture byCorynebacterium diphtheriae |
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Insight into the autoproteolysis mechanism of the RsgI9 anti-σ factorfrom Clostridium thermocellum (ref. 124) |
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2023 |
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The Shr receptor from Streptococcus pyogenes uses a 'cap and release'mechanism to acquire heme-iron from human hemoglobin (ref. 120) |
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Development and atomic structure of a new fluorescence-based sensorto probe heme transfer in bacterial pathogens (ref. 123) |
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The basal and major pilins in the Corynebacterium diphtheriae SpaA pilusadopt similar structures that competitively react with the pilin polymerase(ref. 121) |
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2022 |
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Insight into the molecular basis of substrate recognition by thewall teichoic acid glycosyltransferase TagA (ref. 117) |
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The structure of the Clostridium thermocellum RsgI9 ectodomainprovides insight into the mechanism of biomass sensing (ref. 118) |
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2021 |
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Sortase-assembled pili in Corynebacterium diphtheriae are built usinga latch mechanism (ref. 115) |
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2019 |
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Structure and mechanism of LcpA, a phosphotransferase that mediatesglycosylation of a Gram-positive bacterial cell wall-anchored protein(ref. 105) |
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2018 |
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The Streptococcus pyogenes Shr protein captures human hemoglobinusing two structurally unique binding domains (ref.104) |
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2017 |
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NMR structure-based optimization of pyridazinone classStaphylococcus aureus Sortase A inhibitors (ref. 93) |
2016 |
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Crystal Structure of the Streptomyces coelicolor Sortase E1Transpeptidase Provides Insight into the Binding Mode ofthe Novel Class E Sorting Signal (ref. 92)
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The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdHProtein from Staphylococcus aureus Suggests That It AdaptivelyRecognizes Human Hemoglobin. (ref. 83) |
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2015 |
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Solution structure of the PhoP DNA-binding domain fromMycobacterium tuberculosis. (ref. 86) |
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2014 |
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Novel mechanism of hemin capture by Hbp2, the hemoglobin-bindinghemophore from Listeria monocytogenes. (ref. 82) |
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Structural and computational studies of the Staphylococcus aureussortase B-substrate complex reveal a substrate-stabilized oxyanion hole.(ref. 79) |
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2013 |
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Staphylococcus aureus uses a novel multidomain receptor to breakapart human hemoglobin and steal its heme. (ref. 74) |
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2012 |
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Solution structure of the sortase required for efficient productionof infectious Bacillus anthracis spores. (ref. 88) |
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2011 |
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Transient weak protein-protein complexes transfer heme acrossthe cell wall of Staphylococcus aureus. (ref. 68) |
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Solution structure of the sortase enzyme from Bacillus anthraciscontains a novel active site architecture (ref. 62) |
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Structure of the sortase-substrate complex fromStaphylococcus aureus (ref. 59) |
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NMR structure of the amino-terminal domain of thelambda integrase protein in complex with DNA (ref. 60) |
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2008 |
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Structure of the IsdC-ZnPPIX complex (ref. 56) |
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2007 |
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Crystal structure of the cooperative Xis-DNA complex (ref. 51) |
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NMR structure of the ORF1 RNA binding domain from LINE-1 (ref. 54) |
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2006 |
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NMR structure of the IsdH hemoglobin receptor (ref. 49) |
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2005 |
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NMR structure of the Tn916 Xis protein (ref. 44) |
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Crystal structure of single Xis-DNA complex (ref. 41) |
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2002 |
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NMR structure of the ARID-DNA complex (ref. 31) |
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NMR structure of the lambda integrase DNA binding domain (ref. 32) |
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NMR structure of the lambda Xis protein (ref. 34) |
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2001 |
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NMR structure of the Mu Repressor-DNA complex (ref. 29) |
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NMR structure of Sortase (ref. 26) |
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