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A minimal C-terminal helix in the RPGR BD is sufficient for CID binding and intercalates into the CID helical bundle through a conserved aromatic network. (A) Domain organization of human TTLL5 and RPGR. TTL catalytic core, blue; cMTBD, maroon; CID, green. RCC1-like β-propeller domain in RPGR, yellow, with each repeat shown as a separate propeller blade. <t>Sequence</t> for the minimal BD peptide required for TTLL5 targeting to RPGR shown in magenta at the top. (B) ITC measurements of WT miniBD peptide titrated into CID. Best fit of n = 2 independent experimental replicates. (C) 2.8-Å X-ray crystal structure of human TTLL5 CID in complex with human RPGR miniBD shown in cartoon representation; CID, green; RPGR, magenta. (D and E) Key conserved hydrophobic interactions at the CID–BD interface. Solid black boxes around residue labels designate disease-associated mutations, dashed boxes designate mutations without disease annotation in the ClinVar database that we predict are pathogenic based on our structure. RPGR and TTLL5 are colored as in B; H-bonds are shown as dashed lines.
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A minimal C-terminal helix in the RPGR BD is sufficient for CID binding and intercalates into the CID helical bundle through a conserved aromatic network. (A) Domain organization of human TTLL5 and RPGR. TTL catalytic core, blue; cMTBD, maroon; CID, green. RCC1-like β-propeller domain in RPGR, yellow, with each repeat shown as a separate propeller blade. Sequence for the minimal BD peptide required for TTLL5 targeting to RPGR shown in magenta at the top. (B) ITC measurements of WT miniBD peptide titrated into CID. Best fit of n = 2 independent experimental replicates. (C) 2.8-Å X-ray crystal structure of human TTLL5 CID in complex with human RPGR miniBD shown in cartoon representation; CID, green; RPGR, magenta. (D and E) Key conserved hydrophobic interactions at the CID–BD interface. Solid black boxes around residue labels designate disease-associated mutations, dashed boxes designate mutations without disease annotation in the ClinVar database that we predict are pathogenic based on our structure. RPGR and TTLL5 are colored as in B; H-bonds are shown as dashed lines.

Journal: The Journal of Cell Biology

Article Title: Insights into retinal disease and non-tubulin glutamylation from a RPGR–TTLL5 complex structure

doi: 10.1083/jcb.202508020

Figure Lengend Snippet: A minimal C-terminal helix in the RPGR BD is sufficient for CID binding and intercalates into the CID helical bundle through a conserved aromatic network. (A) Domain organization of human TTLL5 and RPGR. TTL catalytic core, blue; cMTBD, maroon; CID, green. RCC1-like β-propeller domain in RPGR, yellow, with each repeat shown as a separate propeller blade. Sequence for the minimal BD peptide required for TTLL5 targeting to RPGR shown in magenta at the top. (B) ITC measurements of WT miniBD peptide titrated into CID. Best fit of n = 2 independent experimental replicates. (C) 2.8-Å X-ray crystal structure of human TTLL5 CID in complex with human RPGR miniBD shown in cartoon representation; CID, green; RPGR, magenta. (D and E) Key conserved hydrophobic interactions at the CID–BD interface. Solid black boxes around residue labels designate disease-associated mutations, dashed boxes designate mutations without disease annotation in the ClinVar database that we predict are pathogenic based on our structure. RPGR and TTLL5 are colored as in B; H-bonds are shown as dashed lines.

Article Snippet: Vectors were sequenced by Psomagen standard Sanger sequencing service.

Techniques: Binding Assay, Sequencing, Residue

Multiple sequence alignment of vertebrate TTLL5 CID and RPGR BD. (A) TTLL5 CID. (B) RPGR miniBD. Secondary structure elements indicated above the sequence and based on our X-ray crystal structure of the complex; gaps of disordered, unmodeled residues are indicated by a dotted line. Hydrophobic residues at the CID–BD interface indicated with blue boxes. Residues mutated for ITC experiments indicated with black arrows above the sequence.

Journal: The Journal of Cell Biology

Article Title: Insights into retinal disease and non-tubulin glutamylation from a RPGR–TTLL5 complex structure

doi: 10.1083/jcb.202508020

Figure Lengend Snippet: Multiple sequence alignment of vertebrate TTLL5 CID and RPGR BD. (A) TTLL5 CID. (B) RPGR miniBD. Secondary structure elements indicated above the sequence and based on our X-ray crystal structure of the complex; gaps of disordered, unmodeled residues are indicated by a dotted line. Hydrophobic residues at the CID–BD interface indicated with blue boxes. Residues mutated for ITC experiments indicated with black arrows above the sequence.

Article Snippet: Vectors were sequenced by Psomagen standard Sanger sequencing service.

Techniques: Sequencing