4YF2

Crystal structure of mouse sperm C-type lysozyme-like protein 1

「2GOI」から置き換えられました

4YF2 の概要

• エントリーDOI: 10.2210/pdb4yf2/pdb
• 分子名称: Sperm acrosome membrane-associated protein 3 (2 entities in total)
• 機能のキーワード: cell adhesion, sugar binding protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 47702.27

構造登録者

Zheng, H.,Mandal, A.,Shumilin, I.A.,Shabalin, I.G.,Herr, J.C.,Minor, W. (登録日: 2015-02-24, 公開日: 2015-03-11, 最終更新日: 2024-11-13)

主引用文献

Zheng, H.,Mandal, A.,Shumilin, I.A.,Chordia, M.D.,Panneerdoss, S.,Herr, J.C.,Minor, W.
Sperm Lysozyme-Like Protein 1 (SLLP1), an intra-acrosomal oolemmal-binding sperm protein, reveals filamentous organization in protein crystal form.
Andrology, 3:756-771, 2015

PubMed Abstract: Sperm lysozyme-like protein 1 (SLLP1) is one of the lysozyme-like proteins predominantly expressed in mammalian testes that lacks bacteriolytic activity, localizes in the sperm acrosome, and exhibits high affinity for an oolemmal receptor, SAS1B. The crystal structure of mouse SLLP1 (mSLLP1) was determined at 2.15 Å resolution. mSLLP1 monomer adopts a structural fold similar to that of chicken/mouse lysozymes retaining all four canonical disulfide bonds. mSLLP1 is distinct from c-lysozyme by substituting two essential catalytic residues (E35T/D52N), exhibiting different surface charge distribution, and by forming helical filaments approximately 75 Å in diameter with a 25 Å central pore comprised of six monomers per helix turn repeating every 33 Å. Cross-species alignment of all reported SLLP1 sequences revealed a set of invariant surface regions comprising a characteristic fingerprint uniquely identifying SLLP1 from other c-lysozyme family members. The fingerprint surface regions reside around the lips of the putative glycan-binding groove including three polar residues (Y33/E46/H113). A flexible salt bridge (E46-R61) was observed covering the glycan-binding groove. The conservation of these regions may be linked to their involvement in oolemmal protein binding. Interaction between SLLP1 monomer and its oolemmal receptor SAS1B was modeled using protein-protein docking algorithms, utilizing the SLLP1 fingerprint regions along with the SAS1B conserved surface regions. This computational model revealed complementarity between the conserved SLLP1/SAS1B interacting surfaces supporting the experimentally observed SLLP1/SAS1B interaction involved in fertilization.

PubMed: 26198801
DOI: 10.1111/andr.12057

実験手法

X-RAY DIFFRACTION (2.15 Å)