5WLS
Crystal Structure of a Pollen Receptor Kinase 3
Summary for 5WLS
| Entry DOI | 10.2210/pdb5wls/pdb |
| Descriptor | Pollen receptor-like kinase 3, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | pollen receptor kinase, leucine rich repeat, extracellular domain, receptor like kinase, plant protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 47537.93 |
| Authors | Xu, G.,Chakraborty, S.,Pan, H. (deposition date: 2017-07-27, release date: 2018-06-06, Last modification date: 2024-10-30) |
| Primary citation | Chakraborty, S.,Pan, H.,Tang, Q.,Woolard, C.,Xu, G. The Extracellular Domain of Pollen Receptor Kinase 3 is structurally similar to the SERK family of co-receptors. Sci Rep, 8:2796-2796, 2018 Cited by PubMed Abstract: During reproduction in flowering plants, the male gametophyte delivers an immotile male gamete to the female gametophyte in the pistil by formation of pollen tubes. In Arabidopsis thaliana, two synergid cells situated on either side of the egg cell produce cysteine-rich chemoattractant peptide LURE that guides the pollen tube to the female gametophyte for sexual reproduction. Recently, in Arabidopsis thaliana, Pollen Receptor Kinase 3 (PRK3), along with PRK1, PRK6, and PRK8, have been predicted to be the receptors responsible for sensing LURE. These receptors belong to the Leucine Rich Repeat Receptor Like Kinases (LRR-RLKs), the largest family of receptor kinases found in Arabidopsis thaliana. How PRKs regulate the growth and development of the pollen tube remains elusive. In order to better understand the PRK-mediated signaling mechanism in pollen tube growth and guidance, we have determined the crystal structure of the extracellular domain (ecd) of PRK3 at 2.5 Å, which resembles the SERK family of plant co-receptors. The structure of ecdPRK3 is composed of a conserved surface that coincides with the conserved receptor-binding surface of the SERK family of co-receptors. Our structural analyses of PRK3 have provided a template for future functional studies of the PRK family of LRR-RLK receptors in the regulation of pollen tube development. PubMed: 29434276DOI: 10.1038/s41598-018-21218-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.496 Å) |
Structure validation
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