STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOS

An improved 2.9 Å resolution electron density map of lobster holo-D-glyceraldehyde-3-phosphate dehydrogenase was computed using two heavy atom isomorphous derivatives. The map, averaged over the Q molecular 2-fold axis, revealed possible asymmetry between subunits around the active center. Author Dino Moras described conformational differences in adenine ribose and cysteine-histidine associations across the R axis-related subunits.

Use Cases

• Modeling protein subunit asymmetry based on electron density differences described in the study.
• Analyzing active center conformational states based on the anti and syn adenine conformations mentioned.
• Investigating hydrogen bonding patterns in enzyme active sites based on the described ribose 3'-hydroxyl interactions.
• Studying the relationship between cysteine-149 and histidine-176 proximity across different subunits as suggested by the data.

Strengths

• Data is derived from an improved electron density map computed to 2.9 Å resolution.
• Analysis is based on two heavy atom isomorphous derivatives, a specific methodological detail.
• The description provides concrete structural interpretations, such as differing ribose conformations (C-2' endo vs. C-3' endo).

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

Dino Moras via paperswithcode

Collection Method

X-ray crystallography data from lobster holo-D-glyceraldehyde-3-phosphate dehydrogenase crystals, processed with electron density map computation and difference mapping.