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5ZXA

Crystal structure of fibronectin-binding protein Apa mutant from Mycobacterium tuberculosis

Summary for 5ZXA
Entry DOI10.2210/pdb5zxa/pdb
DescriptorAlanine and proline-rich secreted protein Apa, MERCURY (II) ION, GLYCEROL, ... (4 entities in total)
Functional Keywordssubstrate binding, cyclolavandulyl diphosphate synthase, inhibitor, protein binding
Biological sourceMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Total number of polymer chains1
Total formula weight33066.27
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 citationKuo, 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: 31175911
DOI: 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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