Author: Lang, Dorothy M.; Zemla, A. T.; Zhou, C. L. Ecale
Title: Highly similar structural frames link the template tunnel and NTP entry tunnel to the exterior surface in RNA-dependent RNA polymerases Document date: 2012_12_25
ID: s90geszi_96
Snippet: The position of the hmB within the tertiary structure of PV is illustrated in Figure 5B . The N-terminal residue is at the exterior surface of the protein. The N-terminal segment is a classical b-hairpin protein structure that is folded back on itself and is almost entirely exposed on a surface nearly perpendicular to the face of the protein that contains the N-terminal residue ( Figure 5C ). The base of the loop transitions to Motif B at the tem.....
Document: The position of the hmB within the tertiary structure of PV is illustrated in Figure 5B . The N-terminal residue is at the exterior surface of the protein. The N-terminal segment is a classical b-hairpin protein structure that is folded back on itself and is almost entirely exposed on a surface nearly perpendicular to the face of the protein that contains the N-terminal residue ( Figure 5C ). The base of the loop transitions to Motif B at the template tunnel. The C-terminal side of the homomorph extends from the tunnel to the exterior surface of the protein ( Figure 5D ).
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