June 2008 issue
Cover illustration: The hybrid cluster protein from Desulfovibrio vulgaris showing the three domains (p. 665). The hybrid Fe-S cluster lies at the interface of the three domains in the centre of the picture, whilst the cubane Fe-S cluster is bound near the N-terminus of domain1 (coloured in green).
Acta Cryst. (2008). D64, 611-619
The structure of mouse IP-10 shows a novel tetrameric association.
PDB reference: mouse IP-10, 2r3z, r2r3zsf
Acta Cryst. (2008). D64, 620-626
A method of automatically fitting nucleic acid double helices into electron density of high to medium resolution is presented and tested.
Acta Cryst. (2008). D64, 627-635
The 1.25 Å resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis
The crystal structure of M. tuberculosis phosphoribosyl-ATP pyrophosphohydrolase, the second enzyme in the histidine-biosynthetic pathway, is presented. The structural and inferred functional relationships between M. tuberculosis phosphoribosyl-ATP pyrophosphohydrolase and other members of the nucleoside-triphosphate pyrophosphatase-fold family are described.
Acta Cryst. (2008). D64, 636-643
The structure of the Fab fragment f3p4 selected from the HuCAL GOLD library is reported.
PDB reference: Fab fragment f3p4, 2v7n, r2v7nsf
Acta Cryst. (2008). D64, 644-650
Structural analysis of the L-alanoyl-D-glutamate endopeptidase domain of Listeria bacteriophage endolysin Ply500 reveals a new member of the LAS peptidase family
The crystal structure of the enzymatically active domain of Ply500 has been solved at 1.8 Å resolution.
PDB reference: enzymatically active domain of Ply500, 2vo9, r2vo9sf
Acta Cryst. (2008). D64, 651-657
The crystal structure of human α-enolase (hENO1) has been determined for the first time and discloses distinct surface properties despite its high sequence similarities to other enolases. The surface properties provide an insight into its unique activities, including plasmin(ogen) and DNA binding, which are closely related to its roles in numerous diseases such as metastatic cancer, autoimmune disorders, ischaemia and bacterial infection.
PDB reference: human α-enolase, 3b97, r3b97sf
Acta Cryst. (2008). D64, 658-664
An evaluation is made of the protonation states of surface Asp and Glu residues in the C1 domain of cMyBP-C at 1.3 Å resolution. Extrapolations are made of the X-ray diffraction resolution required and/or of the specimen volume required for neutron protein crystallography to determine such states precisely.
PDB reference: cMyBP-C C1 domain, 3cx2, r3cx2sf
Acta Cryst. (2008). D64, 665-674
Structural and functional relationships in the hybrid cluster protein family: structure of the anaerobically purified hybrid cluster protein from Desulfovibrio vulgaris at 1.35 Å resolution
Hybrid cluster proteins (HCP), whose function has yet to be determined, possess a similar fold to carbon monoxide dehydrogenases which also have a related metal–sulfur cluster at the equivalent hybrid cluster position. In HCP the precise nature of the hybrid cluster appears to be dependent on the absence or presence of oxygen during the purification and crystallization procedures.
PDB reference: hybrid cluster protein, 1w9m, r1w9msf
Acta Cryst. (2008). D64, 675-685
Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum
The crystal structures of apo histidinol-phosphate aminotransferase from C. glutamicum, of the internal PLP aldimine adduct and of a pyridoxamine 5-phosphate–enzyme complex were determined at resolutions of 2.2, 2.1 and 1.8 Å, respectively. The residues lining the substrate-binding pocket were studied by site-directed mutagenesis.
PDB references: apo-HisC, 3cq4, r3cq4sf; PMP-HisC, 3cq5, r3cq5sf; PLP-HisC, 3cq6, r3cq6sf
Acta Cryst. (2008). D64, 686-695
Microporous molecular sieves were used as a hetero-epitaxic nucleant for protein crystallization.
Acta Cryst. (2008). D64, 696-699
The crystal structure of an archaeal alanine:glyoxylate aminotransferase which has an amino-acid sequence that shows no similarity to any other known alanine:glyoxylate aminotransferases was determined.
PDB reference: alanine:glyoxylate aminotransferase, 2zc0, r2zc0sf
Acta Cryst. (2008). D64, 700-704
Human Fc fragments containing the L234F/L235E/P331S triple mutation exhibit a dramatic decrease in their binding to several effector molecules (CD64, CD32A, CD16 and C1q). The three-dimensional structure of such a mutated fragment reveals that these broad-ranging functional effects are not caused by major structural rearrangements in the Fc moiety.
PDB reference: human Fc fragment, 3c2s, r3c2ssf