5ZXA
Crystal structure of fibronectin-binding protein Apa mutant from Mycobacterium tuberculosis
Summary for 5ZXA
Entry DOI | 10.2210/pdb5zxa/pdb |
Descriptor | Alanine and proline-rich secreted protein Apa, MERCURY (II) ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | substrate binding, cyclolavandulyl diphosphate synthase, inhibitor, protein binding |
Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Total number of polymer chains | 1 |
Total formula weight | 33066.27 |
Authors | Gao, J.,Liu, W.D.,Chen, C.C.,Guo, R.T. (deposition date: 2018-05-18, release date: 2019-05-29, Last modification date: 2024-03-27) |
Primary citation | Kuo, C.J.,Gao, J.,Huang, J.W.,Ko, T.P.,Zhai, C.,Ma, L.,Liu, W.,Dai, L.,Chang, Y.F.,Chen, T.H.,Hu, Y.,Yu, X.,Guo, R.T.,Chen, C.C. Functional and structural investigations of fibronectin-binding protein Apa from Mycobacterium tuberculosis. Biochim Biophys Acta Gen Subj, 1863:1351-1359, 2019 Cited by PubMed Abstract: Alanine and proline-rich protein (Apa) is a secreted antigen of Mycobacterium spp. which involves in stimulating immune responses and adhering to host cells by binding to fibronectin (Fn). Here, we report the crystal structure of Apa from Mycobacterium tuberculosis (Mtb) and its Fn-binding characteristics. PubMed: 31175911DOI: 10.1016/j.bbagen.2019.06.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.77 Å) |
Structure validation
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