Difference between revisions of "Part:BBa K5246034"
(→‎Experimental characterization)
Line 29: Line 29:
  
 
To sum up, HfsL is most probably a globular family 2 glycosyltransferase, responsible for N-acetyl-D-glucosamine transfer to the acceptor molecule, as is further verified by existing research. [1][2][3]
 
To sum up, HfsL is most probably a globular family 2 glycosyltransferase, responsible for N-acetyl-D-glucosamine transfer to the acceptor molecule, as is further verified by existing research. [1][2][3]
 +
 +
 +
 +
<html lang="en">
 +
<head>
 +
    <meta charset="UTF-8">
 +
    <meta name="viewport" content="width=device-width, initial-scale=1.0">
 +
    <title>Animated Text</title>
 +
    <style>
 +
        @keyframes spin {
 +
            0% { transform: rotate(0deg); }
 +
            100% { transform: rotate(360deg); }
 +
        }
 +
 +
        @keyframes pulse {
 +
            0%, 100% { transform: scale(1); }
 +
            50% { transform: scale(1.2); }
 +
        }
 +
 +
        @keyframes rainbow {
 +
            0% { color: red; }
 +
            14% { color: orange; }
 +
            28% { color: yellow; }
 +
            42% { color: green; }
 +
            57% { color: blue; }
 +
            71% { color: indigo; }
 +
            85% { color: violet; }
 +
            100% { color: red; }
 +
        }
 +
 +
        .animated-text {
 +
            font-size: 2em;
 +
            font-weight: bold;
 +
            display: inline-block;
 +
            animation: spin 5s linear infinite, pulse 2s ease-in-out infinite, rainbow 3s linear infinite;
 +
        }
 +
    </style>
 +
</head>
 +
<body>
 +
    <p class="animated-text">This part needs more characterization</p>
 +
</body>
 +
</html>
  
 
===References===
 
===References===

Revision as of 16:52, 1 October 2024


HB HfsL Glycosyltransferase, 6xHis tag for purification

Introduction

Usage and Biology

TBA

This part also has a non his-tagged variant BBa_K5246024.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 175
  • 1000
    COMPATIBLE WITH RFC[1000]


Experimental characterization

Bioinformatic analysis

CDD analysis showed specific hits in glycosyl transferase family 2. This diverse family transfers sugar from UDP-glucose, UDP-N-acetyl-galactosamine, GDP-mannose, or CDP-abequose to a range of substrates. Protein BLAST further supports these findings and suggests that HfsL is most likely a family 2 glycosyltransferase, which has a domain very similar to the poly-beta-1,6-N-acetyl-D-glucosamine synthase domain of biofilm PGA synthase.

DeepTMHMM analysis suggests that the protein is likely globular and positioned on the inner side of the cell membrane. The AlphaFold 3 structure provides additional evidence supporting its globular shape. A pTM score above 0.5 suggests that the predicted overall structure may closely resemble the true protein fold, while ipTM indicates the accuracy of the subunit positioning within the complex. Values higher than 0.8 represent confident, high-quality predictions.

To sum up, HfsL is most probably a globular family 2 glycosyltransferase, responsible for N-acetyl-D-glucosamine transfer to the acceptor molecule, as is further verified by existing research. [1][2][3]


Animated Text

This part needs more characterization

References

1. Hershey, D.M., Fiebig, A. and Crosson, S. (2019) ‘A genome-wide analysis of adhesion in Caulobacter crescentus identifies new regulatory and biosynthetic components for holdfast assembly’, mBio, 10(1). doi:10.1128/mbio.02273-18.
2. Chepkwony, N.K., Hardy, G.G. and Brun, Y.V. (2022) ‘HFAE is a component of the holdfast anchor complex that tethers the holdfast adhesin to the cell envelope’, Journal of Bacteriology, 204(11). doi:10.1128/jb.00273-22.
3. Chepkwony, N.K., Berne, C. and Brun, Y.V. (2019) ‘Comparative analysis of ionic strength tolerance between freshwater and marine Caulobacterales adhesins’, Journal of Bacteriology, 201(18). doi:10.1128/jb.00061-19.