1. Volume 9, Issue 7, Pages 547-557 (July 2001)
Structure of the UDP-Glucosyltransferase GtfB That Modifies the Heptapeptide Aglycone in the Biosynthesis of Vancomycin Group Antibiotics 
Anne M. Mulichak, Heather C. Losey, Christopher T. Walsh, R.Michael Garavito 
Structure 
Volume 9, Issue 7, Pages (July 2001)
DOI: /S (01)

2. Figure 1
Structure and Glycosylation Pattern of Vancomycin and Chloroeremomycin
The structures of two vancomycin group antibiotics are shown, with the crosslinked amino acids numbered. The sugars are labeled in each structure, and for chloroeremomycin, the enzymes responsible for the glycosyl transfer are shown above the indicated sugar
Structure 2001 9, DOI: ( /S (01) )

3. Figure 2 Views of the GtfB Structure
(a) A backbone representation of GtfB along with the position of the bound sulfate ion (yellow).
(b) A ribbon representation of GtfB highlights the β strands of the Rossmann fold in each domain as well as the residues bordering the disordered regions.
(c) The abrupt end in electron density at Pro139 is shown as it enters the disordered region of the second hypervariable region, following the well-resolved four proline stretch, 136–139.
Figures 2, 4, and 5 were generated using SETOR [38]
Structure 2001 9, DOI: ( /S (01) )

4. Figure 3
Sequence Alignment of Eight GTFs Involved in HPC Glycosylation
The aligned sequences of cGtfB (chloroeremomycin gtfB, CAA ), bGtfB (balhimycin gtfB, CAA ), vGtfE (vancomycin gtfE, AAB ), cGtfC (chloroeremomycin gtfC, CAA ), bGtfC (balhimycin gtfC, CAA ), vGtfD (vancomycin gtfD, AAB ), cGtfA (chloroeremomycin gtfA, CAA ), and bGtfA (balhimycin gtfA, CAA ) show the close relationship between these enzymes. Elements of secondary structure are indicated, and locations of the interdomain linker peptide (blue), the helical tail (pink), glycine-rich regions (yellow), and hypervariable regions (green) are highlighted
Structure 2001 9, DOI: ( /S (01) )

5. Figure 4
Stereo View Showing Ribbon Diagrams of Homologous GtfB, MurG, and T4 β-GT Structures
A high degree of conservation of the β sheets (highlighted in blue) is clearly visible. In the T4 β-GT structure, the bound UDP is shown in red
Structure 2001 9, DOI: ( /S (01) )

6. Figure 5 Stereo Views of the C-Terminal Domains of β-GT and GtfB
(a) The UDP binding site and surrounding residues in β-GT [14], with bound UDP shown in blue. Two of the three arginines that ligand the pyrophosphate in β-GT (Arg191 and Arg269) are shown.
(b) The C-terminal domain of GtfB is shown with the bound sulfate (yellow) sitting at the N-terminal end of the Cα4 helix. The Asp332, the best candidate for the general base, is shown in red
Structure 2001 9, DOI: ( /S (01) )

7. Figure 6
A Sequence Alignment Between More Distantly Related Glycosyltransferases
The region of the highly conserved Gly-rich sequence HHGGAGT (blue box) as well as the strictly conserved Pro323 and the highly conserved Asp 332, the potential catalytic base (asterisk), are highlighted. The sequences referred to are: cgtfB (chloroeremomycin gtfB, CAA ), bgtfB (balhimycin gtfB, CAA ), GtfD (vancomycin gtfD, AAB ), Mtgtf (putative gtf, Mycobacterium tuberculosis, CAB ), Mlgtf (putative gtf, Mycobacterium leprae, AAA ), Martf (rhamnosyltransferase rtfA, Mycobacterium avium, AAD ), Atgtf (putative UDP-glucose:sterol glucosyltransferase, Arabidopsis thaliana, AAD ), EreC (erythromycin gtf eryCIII, Saccharopolyspora erythraea, CAA ), OleG2 (gtf in oleandomycin biosynthesis, Streptomyces antibioticus, CAA ), dnrS (daunosaminyltransferase dnmS, Streptomyces peucetius, AAD ), MurG (UDP-N-acetylglucosaminyltransferase, Escherichia coli, P17443), eryBV (gtf in erythromycin biosynthesis, Saccharopolyspora erythraea, AAB ), dnrH (putative gtf in baumycin biosynthesis, Streptomyces peucetius, AAD ), urdGT1a (gtf in urdamycin A biosynthesis, Streptomyces fradiae, AAF ), and Ugatf (human UDP-glucuronosyltransferase 2B-4 precursor, JN0619)
Structure 2001 9, DOI: ( /S (01) )

8. Figure 7
Molecular Surface Views of the N-Terminal Domain With Proposed Acceptor Binding Site
(a) The stereo view of the empty aglycone site has the surface colored to highlight the locations of Leu102 and Leu103 at the center of the hydrophobic pocket (yellow), aromatic side chains (magenta), disordered peptides (green), and the interdomain linker peptide (cyan).
(b) A close-up view of the aglycone site shows the approximate position of bound UDP-glucose as derived from superposition of the conserved β sheet structure of the C-terminal domain with that of the β-GT binary complex with UDP (see text). A model for the possible position of the vancomycin aglycone bound on the surface of the N-terminal domain is also shown. The phenolic oxygen of the 4-OH-Phegly4 can be positioned near the C1′ atom of the glucosyl ring, as would be required for hexose transfer.
The figure was generated using SPOCK [39] and RASTER3D [40]
Structure 2001 9, DOI: ( /S (01) )