Crystal Structure of the Hemed1Biosynthesis Enzyme NirE in Complex with Its Substrate Reveals New Insights into the Catalytic Mechanism ofS-Adenosyl-l-methionine-dependent Uroporphyrinogen III Methyltransferases

Integration, scaling, space-group assignment and post-refinement

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

XDS

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structure and function of enzymes in heme biosynthesis

(2010) Gunhild Layer et al.   PROTEIN SCIENCE

Functional characterization of the early steps of tetrapyrrole biosynthesis and modification inDesulfovibrio vulgarisHildenborough

(2009) Susana A. L. Lobo et al.   BIOCHEMICAL JOURNAL

d1 haem biogenesis - assessing the roles of three nir gene products

(2009) Richard S. Zajicek et al.   FEBS Journal

The Pseudomonas aeruginosa nirE gene encodes the S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase required for heme d1 biosynthesis

(2009) Sonja Storbeck et al.   FEBS Journal

Discrimination between Closely Related Cellular Metabolites by the SAM-I Riboswitch

(2009) Rebecca K. Montange et al.   JOURNAL OF MOLECULAR BIOLOGY

Structure and Mechanistic Implications of a Uroporphyrinogen III Synthase−Product Complex†‡

(2008) Heidi L. Schubert et al.   BIOCHEMISTRY

Geometric characteristics of hydrogen bonds involving sulfur atoms in proteins

(2008) Peng Zhou et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS